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Volumn 3, Issue 2, 2009, Pages

The nucleoid: An overview

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EID: 84941421899     PISSN: None     EISSN: 23246200     Source Type: Journal    
DOI: 10.1128/ecosalplus.2.6     Document Type: Article
Times cited : (18)

References (334)
  • 2
    • 0001436751 scopus 로고    scopus 로고
    • The nucleoid
    • Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, and Umbarger HE (ed), American Society for Microbiology, Washington, DC
    • Pettijohn DE. 1996. The nucleoid, p 158-166 In Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 158-166
    • Pettijohn, D.E.1
  • 3
    • 0002213084 scopus 로고
    • The nucleoid
    • Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, and Umbarger HE (ed), American Society for Microbiology, Washington, DC
    • Drlica K. 1987. The nucleoid, p 91-103. In Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. American Society for Microbiology, Washington, DC.
    • (1987) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 91-103
    • Drlica, K.1
  • 4
    • 0016844463 scopus 로고
    • Isolation and properties of the transcription complex of Escherichia coli RNA polymerase
    • Naito S, Ishihama A. 1975. Isolation and properties of the transcription complex of Escherichia coli RNA polymerase. Biochim Biophys Acta 402:88-104.
    • (1975) Biochim Biophys Acta , vol.402 , pp. 88-104
    • Naito, S.1    Ishihama, A.2
  • 5
    • 0015928164 scopus 로고
    • Transcriptive complex: Isolation by cesium sulfate centrifugation
    • Naito S, Ishihama A. 1973. Transcriptive complex: Isolation by cesium sulfate centrifugation. Biochem Biophys Res Commun 51:323-330.
    • (1973) Biochem Biophys Res Commun , vol.51 , pp. 323-330
    • Naito, S.1    Ishihama, A.2
  • 6
    • 0030847091 scopus 로고    scopus 로고
    • Isolation and characterization of spermidine nucleoids from Escherichia coli
    • Murphy L, Zimmerman SB. 1997. Isolation and characterization of spermidine nucleoids from Escherichia coli. J Struct Biol 119:321-335.
    • (1997) J Struct Biol , vol.119 , pp. 321-335
    • Murphy, L.1    Zimmerman, S.B.2
  • 7
    • 0030875091 scopus 로고    scopus 로고
    • Stabilization of compact spermidine nucleoids from Escherichia coli under crowded conditions: implications for in vivo nucleoid structure
    • Murphy LD, Zimmerman SB. 1997. Stabilization of compact spermidine nucleoids from Escherichia coli under crowded conditions: implications for in vivo nucleoid structure. J Struct Biol 119:336-346.
    • (1997) J Struct Biol , vol.119 , pp. 336-346
    • Murphy, L.D.1    Zimmerman, S.B.2
  • 8
    • 0034879714 scopus 로고    scopus 로고
    • Release of compact nucleoids with characteristic shape from Escherichia coli
    • Zimmerman SB, Murphy LD. 2001. Release of compact nucleoids with characteristic shape from Escherichia coli. J Bacteriol 183:5041-5049.
    • (2001) J Bacteriol , vol.183 , pp. 5041-5049
    • Zimmerman, S.B.1    Murphy, L.D.2
  • 9
    • 2942515131 scopus 로고    scopus 로고
    • Studies on the compaction of isolated nucleoids from Escherichia coli
    • Zimmerman S. 2004. Studies on the compaction of isolated nucleoids from Escherichia coli. J Struct Biol 147:146-158.
    • (2004) J Struct Biol , vol.147 , pp. 146-158
    • Zimmerman, S.1
  • 10
    • 31344453142 scopus 로고    scopus 로고
    • Cooperative transition of isolated Escherichia coli nucleoids: Implications for the nucleoid as a cellular phase
    • Zimmerman S. 2006. Cooperative transition of isolated Escherichia coli nucleoids: Implications for the nucleoid as a cellular phase. J Struct Biol 153:160-185.
    • (2006) J Struct Biol , vol.153 , pp. 160-185
    • Zimmerman, S.1
  • 12
    • 0035782861 scopus 로고    scopus 로고
    • Polymer-mediated compaction and internal dynamics of isolated Escherichia coli nucleoids
    • Cunha S, Woldringh CL, Odijk T. 2001. Polymer-mediated compaction and internal dynamics of isolated Escherichia coli nucleoids. J Struct Biol 136:53-66.
    • (2001) J Struct Biol , vol.136 , pp. 53-66
    • Cunha, S.1    Woldringh, C.L.2    Odijk, T.3
  • 13
    • 0026344818 scopus 로고
    • Estimation of macromolecular concentrations and excluded volumes for the cytoplasm of Escherichia coli
    • Zimmerman SB, Trach SO. 1991. Estimation of macromolecular concentrations and excluded volumes for the cytoplasm of Escherichia coli. J Mol Biol 232:599-620.
    • (1991) J Mol Biol , vol.232 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 14
    • 0035783032 scopus 로고    scopus 로고
    • A limited loss of DNA compaction accompanying the release of cytoplasm from cells of Escherichia coli
    • Murphy L, Zimmerman SB. 2001. A limited loss of DNA compaction accompanying the release of cytoplasm from cells of Escherichia coli. J Struct Biol 133:75-86.
    • (2001) J Struct Biol , vol.133 , pp. 75-86
    • Murphy, L.1    Zimmerman, S.B.2
  • 15
    • 0037403499 scopus 로고    scopus 로고
    • Underlying regularity in the shapes of nucleoids of Escherichia coli: implications for nucleoid organization and partition
    • Zimmerman S. 2003. Underlying regularity in the shapes of nucleoids of Escherichia coli: implications for nucleoid organization and partition. J Struct Biol 142:256-265.
    • (2003) J Struct Biol , vol.142 , pp. 256-265
    • Zimmerman, S.1
  • 16
    • 33749177128 scopus 로고    scopus 로고
    • The Escherichia coli chromosome is organized with the left and right chromosome arms in separate cell halves
    • Nielsen HJ, Ottesen JR, Youngren B, Austin SJ, Hansen FG. 2006. The Escherichia coli chromosome is organized with the left and right chromosome arms in separate cell halves. Mol Microbiol 62:331-338.
    • (2006) Mol Microbiol , vol.62 , pp. 331-338
    • Nielsen, H.J.1    Ottesen, J.R.2    Youngren, B.3    Austin, S.J.4    Hansen, F.G.5
  • 17
    • 0025916452 scopus 로고
    • Functional consequences of improved structural information on bacterial nucleoids
    • Kellenberger E. 1991. Functional consequences of improved structural information on bacterial nucleoids. Res Microbiol 142:229-238.
    • (1991) Res Microbiol , vol.142 , pp. 229-238
    • Kellenberger, E.1
  • 18
    • 0000097378 scopus 로고
    • Intracellular organization of the bacterial genome
    • Drlica K and Riley M (ed), American Society for Microbiology, Washington, DC
    • Kellenberger E. 1990. Intracellular organization of the bacterial genome, p 173-186. In Drlica K and Riley M (ed), The Bacterial Chromosome. American Society for Microbiology, Washington, DC.
    • (1990) The Bacterial Chromosome , pp. 173-186
    • Kellenberger, E.1
  • 19
    • 0025808921 scopus 로고
    • Coralline shape of the bacterial nucleoid after cryofization
    • Bohrmann B, Villiger W, Johnson R, Kellenberger E. 1991. Coralline shape of the bacterial nucleoid after cryofization. J Bacteriol 173:3149-3158.
    • (1991) J Bacteriol , vol.173 , pp. 3149-3158
    • Bohrmann, B.1    Villiger, W.2    Johnson, R.3    Kellenberger, E.4
  • 20
  • 21
    • 9144264275 scopus 로고    scopus 로고
    • Macrodomain organization of the Escherichia coli chromosome
    • Valens M, Penaud S, Rossignol M, Cornet F, Boccard F. 2004. Macrodomain organization of the Escherichia coli chromosome. EMBO J 23:4330-4341.
    • (2004) EMBO J , vol.23 , pp. 4330-4341
    • Valens, M.1    Penaud, S.2    Rossignol, M.3    Cornet, F.4    Boccard, F.5
  • 22
    • 3142774839 scopus 로고    scopus 로고
    • Topological domain structure of the Escherichia coli chromosome
    • Postow L, Hardy CD, Arsuage J, Cozzarelli NR. 2004. Topological domain structure of the Escherichia coli chromosome. Genes Dev 18:1766-1779.
    • (2004) Genes Dev , vol.18 , pp. 1766-1779
    • Postow, L.1    Hardy, C.D.2    Arsuage, J.3    Cozzarelli, N.R.4
  • 23
    • 0041853574 scopus 로고    scopus 로고
    • Bacterial chromosome dynamics
    • Sherratt DJ. 2003. Bacterial chromosome dynamics. Science 301: 780-785.
    • (2003) Science , vol.301 , pp. 780-785
    • Sherratt, D.J.1
  • 24
    • 0034650256 scopus 로고    scopus 로고
    • Dynamic organization of chromosomal DNA in Escherichia coli
    • Niki H, Yamanaka K, Hiraga S. 2000. Dynamic organization of chromosomal DNA in Escherichia coli. Genes Dev 14:212-223.
    • (2000) Genes Dev , vol.14 , pp. 212-223
    • Niki, H.1    Yamanaka, K.2    Hiraga, S.3
  • 25
    • 33750495828 scopus 로고    scopus 로고
    • Organization of the Escherichia coli chromosome into macrodomains and its possible functional implications
    • Espeli O, Boccard F. 2006. Organization of the Escherichia coli chromosome into macrodomains and its possible functional implications. J Struct Biol 156:304-310.
    • (2006) J Struct Biol , vol.156 , pp. 304-310
    • Espeli, O.1    Boccard, F.2
  • 26
    • 44249103292 scopus 로고    scopus 로고
    • DNA dynamics vary according to macrodomain topography in the E. coli chromosome
    • Espeli O, Merchier R, Boccard F. 2008. DNA dynamics vary according to macrodomain topography in the E. coli chromosome. Mol Microbiol 68:1418-1427.
    • (2008) Mol Microbiol , vol.68 , pp. 1418-1427
    • Espeli, O.1    Merchier, R.2    Boccard, F.3
  • 27
    • 54949146519 scopus 로고    scopus 로고
    • The MatP/matS site-specific system organizes the terminus region of the E. coli chromosome into a macrodomain
    • Mercier R, Petit MA, Schbath S, Robin S, El Karoui M, Boccard F, Espeli O. 2008. The MatP/matS site-specific system organizes the terminus region of the E. coli chromosome into a macrodomain. Cell 135:475-485.
    • (2008) Cell , vol.135 , pp. 475-485
    • Mercier, R.1    Petit, M.A.2    Schbath, S.3    Robin, S.4    El Karoui, M.5    Boccard, F.6    Espeli, O.7
  • 28
    • 0034766158 scopus 로고    scopus 로고
    • The looped domain organization of the nucleoid in histone-like protein defective Escherichia coli
    • Brunetti R, Proseda G, Beghetto E, Colonna B, Micheli G. 2001. The looped domain organization of the nucleoid in histone-like protein defective Escherichia coli. Biochemie 83:873-882.
    • (2001) Biochemie , vol.83 , pp. 873-882
    • Brunetti, R.1    Proseda, G.2    Beghetto, E.3    Colonna, B.4    Micheli, G.5
  • 29
    • 0343240577 scopus 로고
    • Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling
    • Sinden RR, Pettijohn DE. 1981. Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling. Proc Natl Acad Sci USA 78:224-228.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 224-228
    • Sinden, R.R.1    Pettijohn, D.E.2
  • 30
    • 0031712188 scopus 로고    scopus 로고
    • Gyrase and topo IV modulate chromosome domain size in vivo
    • Staczek P, Higgins NP. 1998. Gyrase and topo IV modulate chromosome domain size in vivo. Mol Microbiol 29:1435-1448.
    • (1998) Mol Microbiol , vol.29 , pp. 1435-1448
    • Staczek, P.1    Higgins, N.P.2
  • 31
    • 0015506478 scopus 로고
    • On the structure of the folded chromosome of Escherichia coli
    • Worcel A, Burgi E. 1972. On the structure of the folded chromosome of Escherichia coli. J Mol Biol 71:127-147.
    • (1972) J Mol Biol , vol.71 , pp. 127-147
    • Worcel, A.1    Burgi, E.2
  • 32
    • 33745179903 scopus 로고    scopus 로고
    • Distribution of gyrase and topoisomerase IV on bacterial nucleoid: implications for nucleoid organization
    • Hsu, Y-Chung H, M-W, T-Li K. 2006. Distribution of gyrase and topoisomerase IV on bacterial nucleoid: implications for nucleoid organization. Nucleic Acids Res 34:3128-3138.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3128-3138
    • Hsu, Y.H.1    Chung, M.-W.2    Li, T.K.3
  • 34
    • 0030909920 scopus 로고    scopus 로고
    • The bacterial nucleoid visualized by fluorescence microscopy of cells lysed within agarose: comparison of Escherichia coli and spirochetes of the genus Borrelia
    • Hinnebusch BJ, Bendich AJ. 1997. The bacterial nucleoid visualized by fluorescence microscopy of cells lysed within agarose: comparison of Escherichia coli and spirochetes of the genus Borrelia. J Bacteriol 179:2228-2237.
    • (1997) J Bacteriol , vol.179 , pp. 2228-2237
    • Hinnebusch, B.J.1    Bendich, A.J.2
  • 35
    • 0001415964 scopus 로고
    • The pitch of chromatin DNA is reflected in its nucleotide sequence
    • Trifonov EN, Sussman JI. 1980. The pitch of chromatin DNA is reflected in its nucleotide sequence. Proc Natl Acad SciUSA 77:3816-3820.
    • (1980) Proc Natl Acad SciUSA , vol.77 , pp. 3816-3820
    • Trifonov, E.N.1    Sussman, J.I.2
  • 37
    • 0023750111 scopus 로고
    • Rearrangement of the bacterial chromosome: forbidden inversions
    • Segall A, Mahan MJ, Roth JR. 1988. Rearrangement of the bacterial chromosome: forbidden inversions. Science 241:1314-1318.
    • (1988) Science , vol.241 , pp. 1314-1318
    • Segall, A.1    Mahan, M.J.2    Roth, J.R.3
  • 38
    • 0018824063 scopus 로고
    • Supercoils in prokaryotic DNA restrained in vivo
    • Pettijohn D, Pfenninger O. 1980. Supercoils in prokaryotic DNA restrained in vivo. Proc Natl Acad Sci USA 77:1331-1335.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1331-1335
    • Pettijohn, D.1    Pfenninger, O.2
  • 39
    • 0023413620 scopus 로고
    • Histonelike proteins of bacteria
    • Drlica K, Rouviere-Yanif J. 1987. Histonelike proteins of bacteria. Microbiol Rev 51:301-319.
    • (1987) Microbiol Rev , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yanif, J.2
  • 40
    • 0025633561 scopus 로고
    • Transcription regulates oxolinic acid-induced DNA gyrase cleavage at specific sites on the E. coli chromosome
    • Condemine G, Smith CL. 1990. Transcription regulates oxolinic acid-induced DNA gyrase cleavage at specific sites on the E. coli chromosome. Nucleic Acids Res 18:7389-7396.
    • (1990) Nucleic Acids Res , vol.18 , pp. 7389-7396
    • Condemine, G.1    Smith, C.L.2
  • 41
    • 84921182959 scopus 로고
    • Electrophoretic analysis of large DNA: application to the structure and dynamics of the Escherichia coli chromosome
    • Drlica K and Riley M (ed), American Society for Microbiology, Washington, DC
    • Smith CL, Condemine G, Ringquist S. 1990. Electrophoretic analysis of large DNA: application to the structure and dynamics of the Escherichia coli chromosome, p 205-210. In Drlica K and Riley M (ed), The Bacterial Chromosome. American Society for Microbiology, Washington, DC.
    • (1990) The Bacterial Chromosome , pp. 205-210
    • Smith, C.L.1    Condemine, G.2    Ringquist, S.3
  • 42
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi E, Lutkenhaus J. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature 354:161-167.
    • (1991) Nature , vol.354 , pp. 161-167
    • Bi, E.1    Lutkenhaus, J.2
  • 43
    • 0017894437 scopus 로고
    • Folded chromosome of vegetative Bacillus subtilis: composition and properties
    • Guillen N, Le Hegarat F, Fleury A, Hirschbein L. 1978. Folded chromosome of vegetative Bacillus subtilis: composition and properties. Nucleic Acids Res 5:475-489.
    • (1978) Nucleic Acids Res , vol.5 , pp. 475-489
    • Guillen, N.1    Le Hegarat, F.2    Fleury, A.3    Hirschbein, L.4
  • 44
    • 0026459388 scopus 로고
    • Histone-like proteins are required for cell growth and constraint of supercoils in DNA
    • Yasuzawa K, Hayashi N, Goshima N, Kohno K, Imamoto F, Kano Y. 1992. Histone-like proteins are required for cell growth and constraint of supercoils in DNA. Gene 122:9-12.
    • (1992) Gene , vol.122 , pp. 9-12
    • Yasuzawa, K.1    Hayashi, N.2    Goshima, N.3    Kohno, K.4    Imamoto, F.5    Kano, Y.6
  • 45
    • 34248370213 scopus 로고    scopus 로고
    • Spiral structure of Escherichia coli HUαβ provides foundation for DNA supercoiling
    • Guo F, Adhya S. 2007. Spiral structure of Escherichia coli HUαβ provides foundation for DNA supercoiling. Proc Natl Acad Sci USA 104:4309-4314.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4309-4314
    • Guo, F.1    Adhya, S.2
  • 46
    • 33846025466 scopus 로고    scopus 로고
    • Right-handed DNA supercoiling by an octameric form of histone-like protein HU
    • Kar S, Choi EJ, Guo F, Dimitriadis EK, Kotova SL, Adhya S. 2006. Right-handed DNA supercoiling by an octameric form of histone-like protein HU. J Biol Chem 281:40144-40153.
    • (2006) J Biol Chem , vol.281 , pp. 40144-40153
    • Kar, S.1    Choi, E.J.2    Guo, F.3    Dimitriadis, E.K.4    Kotova, S.L.5    Adhya, S.6
  • 47
    • 0029863159 scopus 로고    scopus 로고
    • Surveying a supercoil domain by using the gamma delta resolution system in Salmonella typhimurium
    • Higgins NP, Yang X, Fu Q, Roth JR. 1996. Surveying a supercoil domain by using the gamma delta resolution system in Salmonella typhimurium. J Bacteriol 178:2825-2835.
    • (1996) J Bacteriol , vol.178 , pp. 2825-2835
    • Higgins, N.P.1    Yang, X.2    Fu, Q.3    Roth, J.R.4
  • 48
    • 1942436944 scopus 로고    scopus 로고
    • Unequal access of chromosomal regions to each other in Salmonella enterica: Use of phage lambda integrase-catalyzed long-range rearrangements as a probe of chromosomal packaging
    • Garcia-Russel N, Hamon T, Le TQ, Amaladas N, Mathewson R, Segall AM. 2004. Unequal access of chromosomal regions to each other in Salmonella enterica: Use of phage lambda integrase-catalyzed long-range rearrangements as a probe of chromosomal packaging. Mol Microbiol 54:329-344.
    • (2004) Mol Microbiol , vol.54 , pp. 329-344
    • Garcia-Russel, N.1    Hamon, T.2    Le, T.Q.3    Amaladas, N.4    Mathewson, R.5    Segall, A.M.6
  • 49
    • 45949129922 scopus 로고
    • Palindromic units: a case of highly repetitive DNA sequences in bacteria
    • Gilson E, Clement J, Perrin D, Hofnung M. 1987. Palindromic units: a case of highly repetitive DNA sequences in bacteria. Trends Genet 3:226-230.
    • (1987) Trends Genet , vol.3 , pp. 226-230
    • Gilson, E.1    Clement, J.2    Perrin, D.3    Hofnung, M.4
  • 50
    • 0021669070 scopus 로고
    • Repetitive extragenic palindromic sequences: a major component of the bacterial genome
    • Stern M, Ames G, Smith N, Robinson E, Higgins C. 1984. Repetitive extragenic palindromic sequences: a major component of the bacterial genome. Cell 37:1015-1026.
    • (1984) Cell , vol.37 , pp. 1015-1026
    • Stern, M.1    Ames, G.2    Smith, N.3    Robinson, E.4    Higgins, C.5
  • 51
    • 0002023387 scopus 로고
    • The family of repetitive extragenic palindromic sequences: interaction with DNA gyrase and histone-like protein HU
    • Drlica K and Riley M (ed), American Society for Microbiology, Washington, DC
    • Yang Y, Ames G. 1990. The family of repetitive extragenic palindromic sequences: interaction with DNA gyrase and histone-like protein HU, p 211-225. In Drlica K and Riley M (ed), The Bacterial Chromosome. American Society for Microbiology, Washington, DC.
    • (1990) The Bacterial Chromosome , pp. 211-225
    • Yang, Y.1    Ames, G.2
  • 52
    • 25144495578 scopus 로고    scopus 로고
    • Organization of supercoil domains and their reorganization by transcription
    • Deng S, Stein RA, Higgins NP. 2005. Organization of supercoil domains and their reorganization by transcription. Mol Microbiol 57:1511-1521.
    • (2005) Mol Microbiol , vol.57 , pp. 1511-1521
    • Deng, S.1    Stein, R.A.2    Higgins, N.P.3
  • 53
    • 0027097480 scopus 로고
    • E. coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities
    • Niki H, Imamura R, Kitaoka M, Yamanaka K, Ogura T, Hiraga H. 1992. E. coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities. EMBO J 11:5101-5109.
    • (1992) EMBO J , vol.11 , pp. 5101-5109
    • Niki, H.1    Imamura, R.2    Kitaoka, M.3    Yamanaka, K.4    Ogura, T.5    Hiraga, H.6
  • 54
    • 0029944542 scopus 로고    scopus 로고
    • Identification of two new genes, mukE and mukF, involved in chromosome partitioning in Escherichia coli
    • Yamanaka K, Ogura T, Niki H, Hiraga S. 1996. Identification of two new genes, mukE and mukF, involved in chromosome partitioning in Escherichia coli. Mol Gen Genet 250:241-251.
    • (1996) Mol Gen Genet , vol.250 , pp. 241-251
    • Yamanaka, K.1    Ogura, T.2    Niki, H.3    Hiraga, S.4
  • 55
    • 0016018740 scopus 로고
    • Electron microscopic studies on the folded chromosome of Escherichia coli
    • Delius H, Worcel A. 1974. Electron microscopic studies on the folded chromosome of Escherichia coli. Cold Spring Harbor Symp Quant Biol 38:53-58.
    • (1974) Cold Spring Harbor Symp Quant Biol , vol.38 , pp. 53-58
    • Delius, H.1    Worcel, A.2
  • 56
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu L, Wang J. 1987. Supercoiling of the DNA template during transcription. Proc Natl Acad Sci USA 84:7024-7027.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7024-7027
    • Liu, L.1    Wang, J.2
  • 57
    • 84959148998 scopus 로고    scopus 로고
    • Bacterial RNA polymerases: the whole story
    • Murakami K, Darst SA. 2003. Bacterial RNA polymerases: the whole story. Curr Opin Struct Biol 325:451-470.
    • (2003) Curr Opin Struct Biol , vol.325 , pp. 451-470
    • Murakami, K.1    Darst, S.A.2
  • 58
    • 0028265920 scopus 로고
    • Assembly of nucleosomes: do multiple assembly factors mean multiple mechanisms?
    • Kaufman PD, Botchn MR. 1994. Assembly of nucleosomes: do multiple assembly factors mean multiple mechanisms? Curr Opin Genet Dev 4:229-235.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 229-235
    • Kaufman, P.D.1    Botchn, M.R.2
  • 59
    • 34250168295 scopus 로고    scopus 로고
    • Rules and regulation in the primary structure of chromatin
    • Rando OJ, Ahmad K. 2007. Rules and regulation in the primary structure of chromatin. Curr Opin Cell Biol 19:250-256.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 250-256
    • Rando, O.J.1    Ahmad, K.2
  • 60
    • 3042660143 scopus 로고    scopus 로고
    • Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy
    • Kim J, Yoshimura SH, Hizume K, Ohniwa RL, Ishihama A, Takeyasu K. 2004. Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy. Nucleic Acids Res 32:1982-1992.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1982-1992
    • Kim, J.1    Yoshimura, S.H.2    Hizume, K.3    Ohniwa, R.L.4    Ishihama, A.5    Takeyasu, K.6
  • 65
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • Azam T, Hiraga S, Ishihama A. 2000. Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes Cells 5:613-626.
    • (2000) Genes Cells , vol.5 , pp. 613-626
    • Azam, T.1    Hiraga, S.2    Ishihama, A.3
  • 66
    • 0025304290 scopus 로고
    • Structure and probable genetic location of a "ribosome modulation factor" associated with 100S ribosomes in stationary-phase Escherichia coli
    • Wada A, Yamazaki Y, Fujita N, Ishihama A. 1990. Structure and probable genetic location of a "ribosome modulation factor" associated with 100S ribosomes in stationary-phase Escherichia coli. Proc Natl Acad Sci USA 87:2657-2661.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2657-2661
    • Wada, A.1    Yamazaki, Y.2    Fujita, N.3    Ishihama, A.4
  • 67
    • 0033021173 scopus 로고    scopus 로고
    • Modulation of the nucleoid, the transcription apparatus, and the translation machinery in bacteria for stationary phase survival
    • Ishihama A. 1999. Modulation of the nucleoid, the transcription apparatus, and the translation machinery in bacteria for stationary phase survival. Genes Cells 4:135-143.
    • (1999) Genes Cells , vol.4 , pp. 135-143
    • Ishihama, A.1
  • 68
    • 0033104294 scopus 로고    scopus 로고
    • Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria
    • Dorman CJ, Hinton JCD, Free A. 1999. Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria. Trends Microbiol 7:124-128.
    • (1999) Trends Microbiol , vol.7 , pp. 124-128
    • Dorman, C.J.1    Hinton, J.C.D.2    Free, A.3
  • 69
    • 0035075425 scopus 로고    scopus 로고
    • Control of transcription by nucleoid proteins
    • McLeod SM, Johnson RC. 2001. Control of transcription by nucleoid proteins. Curr Opin Microbiol 4:152-159.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 152-159
    • McLeod, S.M.1    Johnson, R.C.2
  • 70
    • 0018405881 scopus 로고
    • E. coli DNA binding protein HU forms nucleosome-like structure with circular double-stranded DNA
    • Rouviere-Yaniv J, Yaniv M, Germond JE. 1979. E. coli DNA binding protein HU forms nucleosome-like structure with circular double-stranded DNA. Cell 17:265-274.
    • (1979) Cell , vol.17 , pp. 265-274
    • Rouviere-Yaniv, J.1    Yaniv, M.2    Germond, J.E.3
  • 71
    • 0031573039 scopus 로고    scopus 로고
    • Molecular aspects of the E. coli nucleoid protein, H-NS: a central controller of gene regulatory networks
    • Williams DB, Rimsky S. 1997. Molecular aspects of the E. coli nucleoid protein, H-NS: a central controller of gene regulatory networks. FEMS Microbiol Lett 156:175-185.
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 175-185
    • Williams, D.B.1    Rimsky, S.2
  • 72
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam T, Iwata A, Nishimura A, Ueda S, Ishihama A. 1999. Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J Bacteriol 181:6361-6370.
    • (1999) J Bacteriol , vol.181 , pp. 6361-6370
    • Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 73
    • 0037709369 scopus 로고    scopus 로고
    • Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq
    • Sukhodelets MV, Garges S. 2003. Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq. Biochemistry 42:8022-8034.
    • (2003) Biochemistry , vol.42 , pp. 8022-8034
    • Sukhodelets, M.V.1    Garges, S.2
  • 76
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU cocrystal structures
    • Swinger KK, Lemberg KM, Zhang Y, Rice PA. 2003. Flexible DNA bending in HU cocrystal structures. EMBO J 22:3749-3760.
    • (2003) EMBO J , vol.22 , pp. 3749-3760
    • Swinger, K.K.1    Lemberg, K.M.2    Zhang, Y.3    Rice, P.A.4
  • 77
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex; a protein-induced DNA U-turn
    • Rice PA, Yang S, Mizuuchi K, Nash HA. 1996. Crystal structure of an IHF-DNA complex; a protein-induced DNA U-turn. Cell 87:1295-1306.
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.2    Mizuuchi, K.3    Nash, H.A.4
  • 78
    • 0037315037 scopus 로고    scopus 로고
    • Growth phase-coupled alterations in cell structure and function of Escherichia coli
    • Makinoshima H, Aizawa S, Hayashi H, Miki T, Nishimura A, Ishihama A. 2003. Growth phase-coupled alterations in cell structure and function of Escherichia coli. J Bacteriol 185:1338-1345.
    • (2003) J Bacteriol , vol.185 , pp. 1338-1345
    • Makinoshima, H.1    Aizawa, S.2    Hayashi, H.3    Miki, T.4    Nishimura, A.5    Ishihama, A.6
  • 79
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli: Sequence recognition specificity and DNA binding affinity
    • Azam T, Ishihama A. 1999. Twelve species of the nucleoid-associated protein from Escherichia coli: Sequence recognition specificity and DNA binding affinity. J Biol Chem 274:33105-33113.
    • (1999) J Biol Chem , vol.274 , pp. 33105-33113
    • Azam, T.1    Ishihama, A.2
  • 80
    • 0026620949 scopus 로고
    • Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli
    • Ball CA, Osuna R, Ferguson KC, Johnson RC. 1992. Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli. J Bacteriol 174:8043-8056.
    • (1992) J Bacteriol , vol.174 , pp. 8043-8056
    • Ball, C.A.1    Osuna, R.2    Ferguson, K.C.3    Johnson, R.C.4
  • 81
    • 0028307609 scopus 로고
    • Growth phase variation of integration host factor level in Escherichia coli
    • Ditto MD, Roberts D, Weisberg RA. 1994. Growth phase variation of integration host factor level in Escherichia coli. J Bacteriol 176:3738-3748.
    • (1994) J Bacteriol , vol.176 , pp. 3738-3748
    • Ditto, M.D.1    Roberts, D.2    Weisberg, R.A.3
  • 82
    • 3042522654 scopus 로고    scopus 로고
    • Chromatin dynamics at DNA replication, transcription and repair
    • Ehrenhofer-Murry AE. 2004. Chromatin dynamics at DNA replication, transcription and repair. Eur J Biochem 271:2335-2349.
    • (2004) Eur J Biochem , vol.271 , pp. 2335-2349
    • Ehrenhofer-Murry, A.E.1
  • 83
    • 4644255692 scopus 로고    scopus 로고
    • Chromatin modifiers in transcription and DNA repair
    • Verger A, Crossley M. 2004. Chromatin modifiers in transcription and DNA repair. Cell Mol Life Sci 61:2154-2162.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 2154-2162
    • Verger, A.1    Crossley, M.2
  • 84
    • 0026470852 scopus 로고
    • The Fis protein: it's not just for DNA inversion anymore
    • Finkel SE, Johnson RC. 1992. The Fis protein: it's not just for DNA inversion anymore. Mol Microbiol 6:3257-3265.
    • (1992) Mol Microbiol , vol.6 , pp. 3257-3265
    • Finkel, S.E.1    Johnson, R.C.2
  • 85
    • 0033765113 scopus 로고    scopus 로고
    • Functional modulation of Escherichia coli RNA polymerase
    • Ishihama A. 2000. Functional modulation of Escherichia coli RNA polymerase. Annu Rev Microbiol 54:499-518.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 499-518
    • Ishihama, A.1
  • 86
    • 0025153881 scopus 로고
    • More than just "histone-like" proteins
    • Schmid M. 1990. More than just "histone-like" proteins. Cell 63:451-453.
    • (1990) Cell , vol.63 , pp. 451-453
    • Schmid, M.1
  • 87
    • 0030972952 scopus 로고    scopus 로고
    • H-NS: a modulator of environmentally regulated gene expression
    • Atlung T, Ingmer H. 1997. H-NS: a modulator of environmentally regulated gene expression. Mol Microbiol 24:7-17.
    • (1997) Mol Microbiol , vol.24 , pp. 7-17
    • Atlung, T.1    Ingmer, H.2
  • 88
    • 1842506160 scopus 로고    scopus 로고
    • Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes
    • Barnard AML, Wolfe A, Busby S. 2004. Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes. Curr Opin Microbiol 7:102-108.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 102-108
    • Barnard, A.M.L.1    Wolfe, A.2    Busby, S.3
  • 89
    • 0036274156 scopus 로고    scopus 로고
    • Independent regulation of divergent Escherichia coli nrfA and acsP1 promoters by a nucleoprotein assembly at a shared regulatory region
    • Browning DF, Beatty CM, Wolfe AJ, Cole JA, Busby SJW. 2002. Independent regulation of divergent Escherichia coli nrfA and acsP1 promoters by a nucleoprotein assembly at a shared regulatory region. Mol Microbiol 43:687-701.
    • (2002) Mol Microbiol , vol.43 , pp. 687-701
    • Browning, D.F.1    Beatty, C.M.2    Wolfe, A.J.3    Cole, J.A.4    Busby, S.J.W.5
  • 90
    • 0034085279 scopus 로고    scopus 로고
    • Antagonistic control of the Escherichia coli bgl promoter by Fis and CAP
    • Caramel AM, Schnetz J. 2000. Antagonistic control of the Escherichia coli bgl promoter by Fis and CAP. Mol Microbiol 36:85-92.
    • (2000) Mol Microbiol , vol.36 , pp. 85-92
    • Caramel, A.M.1    Schnetz, J.2
  • 91
    • 0142075908 scopus 로고    scopus 로고
    • The gyr genes of Salmonella serovar typhimurium are repressed by the factor for inversion and stimulation, Fis
    • Keane OM, Dorman CJ. 2003. The gyr genes of Salmonella serovar typhimurium are repressed by the factor for inversion and stimulation, Fis. Mol Genomics 270:56-65.
    • (2003) Mol Genomics , vol.270 , pp. 56-65
    • Keane, O.M.1    Dorman, C.J.2
  • 92
    • 0033404486 scopus 로고    scopus 로고
    • A DNA architectural protein couples cellular physiology and DNA topology in Escherichia coli
    • Schneider R, Travers A, Kutatelandze T, Muskhelishvili G. 1999. A DNA architectural protein couples cellular physiology and DNA topology in Escherichia coli. Mol Microbiol 34:953-964.
    • (1999) Mol Microbiol , vol.34 , pp. 953-964
    • Schneider, R.1    Travers, A.2    Kutatelandze, T.3    Muskhelishvili, G.4
  • 93
    • 0028933852 scopus 로고
    • The Escherichia coli RNA polymerase alpha subunit: structure and function
    • Ebright S, Busby S. 1995. The Escherichia coli RNA polymerase alpha subunit: structure and function. Curr Opin Genet Dev 5:853-859.
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 853-859
    • Ebright, S.1    Busby, S.2
  • 94
    • 0027262508 scopus 로고
    • Protein-protein communication within the transcription apparatus
    • Ishihama A. 1993. Protein-protein communication within the transcription apparatus. J Bacteriol 175:2483-2489.
    • (1993) J Bacteriol , vol.175 , pp. 2483-2489
    • Ishihama, A.1
  • 95
    • 0026471585 scopus 로고
    • Role of the RNA polymerase alpha subunit in transcription activation
    • Ishihama A. 1992. Role of the RNA polymerase alpha subunit in transcription activation. Mol Microbiol 227:3238-3288.
    • (1992) Mol Microbiol , vol.227 , pp. 3238-3288
    • Ishihama, A.1
  • 96
    • 35448941579 scopus 로고    scopus 로고
    • RutR is the uracil/thymine sensing master regulator of a set of genes for synthesis and degradation of pyrimidines
    • Shimada T, Hirao K, Kori A, Yamamoto K, Ishihama A. 2007. RutR is the uracil/thymine sensing master regulator of a set of genes for synthesis and degradation of pyrimidines. Mol Microbiol 66:744-757.
    • (2007) Mol Microbiol , vol.66 , pp. 744-757
    • Shimada, T.1    Hirao, K.2    Kori, A.3    Yamamoto, K.4    Ishihama, A.5
  • 97
    • 0030899580 scopus 로고    scopus 로고
    • Overlapping promoters modulate Fnr-and ArcA-dependent anaerobic transcriptional activation of the focApfloperon in Escherichia coli
    • Kaiser M, Sawers G. 1997. Overlapping promoters modulate Fnr-and ArcA-dependent anaerobic transcriptional activation of the focApfloperon in Escherichia coli. Microbiology 143:775-783.
    • (1997) Microbiology , vol.143 , pp. 775-783
    • Kaiser, M.1    Sawers, G.2
  • 98
    • 3142558001 scopus 로고    scopus 로고
    • Transcriptional and translational regulation of the marRAB multiple antibiotic resistance operon in Escherichia coli
    • Martin RG, Rosner JL. 2004. Transcriptional and translational regulation of the marRAB multiple antibiotic resistance operon in Escherichia coli. Mol Microbiol 53:183-191.
    • (2004) Mol Microbiol , vol.53 , pp. 183-191
    • Martin, R.G.1    Rosner, J.L.2
  • 99
    • 0029884678 scopus 로고    scopus 로고
    • Structure modification induced in the narG promoter by binding of interaction host factor and NarL-P
    • Zhang X, DeMoss JA. 1996. Structure modification induced in the narG promoter by binding of interaction host factor and NarL-P. J Bacteriol 178:3971-3973.
    • (1996) J Bacteriol , vol.178 , pp. 3971-3973
    • Zhang, X.1    DeMoss, J.A.2
  • 100
    • 0026747312 scopus 로고
    • Identification of functional cisacting sequences involved in regulation of narK gene expression in Escherichia coli
    • Bonnefoy V, DeMoss JA. 1992. Identification of functional cisacting sequences involved in regulation of narK gene expression in Escherichia coli. Mol Microbiol 6:3595-3602.
    • (1992) Mol Microbiol , vol.6 , pp. 3595-3602
    • Bonnefoy, V.1    DeMoss, J.A.2
  • 101
    • 22144488494 scopus 로고    scopus 로고
    • Integration of three signals at the Escherichia coli nrf promoter: a role for Fis protein in catabolite repression
    • Browning DF, Grainger DC, Beatty CM, Wolfe AJ, Cole JA, Busby SJW. 2005. Integration of three signals at the Escherichia coli nrf promoter: a role for Fis protein in catabolite repression. Mol Microbiol 57:496-510.
    • (2005) Mol Microbiol , vol.57 , pp. 496-510
    • Browning, D.F.1    Grainger, D.C.2    Beatty, C.M.3    Wolfe, A.J.4    Cole, J.A.5    Busby, S.J.W.6
  • 102
    • 1242341344 scopus 로고    scopus 로고
    • Regulation of ndh expression in Escherichia coli by Fis
    • Jackson L, Blake T, Green J. 2004. Regulation of ndh expression in Escherichia coli by Fis. Microbiology 150:407-413.
    • (2004) Microbiology , vol.150 , pp. 407-413
    • Jackson, L.1    Blake, T.2    Green, J.3
  • 103
    • 33846928720 scopus 로고    scopus 로고
    • Integration of regulatory signals through involvement of multiple global regulators: control of the Escherichia coli gltBDF operon by Lrp, IHF, Crp and ArgR
    • Paul L, Mishra PK, Bluumenthal RM, Matthews RG. 2007. Integration of regulatory signals through involvement of multiple global regulators: control of the Escherichia coli gltBDF operon by Lrp, IHF, Crp and ArgR. BMC Microbiol 7:2.
    • (2007) BMC Microbiol , vol.7 , pp. 2
    • Paul, L.1    Mishra, P.K.2    Bluumenthal, R.M.3    Matthews, R.G.4
  • 104
    • 1942532920 scopus 로고    scopus 로고
    • The histone-like nucleoid structuring protein H-NS represses the Escherichia coli bgl operon downstream of the promoter
    • Dole S, Nagarajavel V, Schnetz K. 2004. The histone-like nucleoid structuring protein H-NS represses the Escherichia coli bgl operon downstream of the promoter. Mol Microbiol 52:589-609.
    • (2004) Mol Microbiol , vol.52 , pp. 589-609
    • Dole, S.1    Nagarajavel, V.2    Schnetz, K.3
  • 105
    • 33745187803 scopus 로고    scopus 로고
    • IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins
    • Yeo W-S, Lee J-H, Lee K-C, Roe H-H. 2006. IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. Mol Microbiol 61:206-218.
    • (2006) Mol Microbiol , vol.61 , pp. 206-218
    • Yeo, W.-S.1    Lee, J.-H.2    Lee, K.-C.3    Roe, H.-H.4
  • 106
    • 0038781388 scopus 로고    scopus 로고
    • Transcriptional expression of Escherichia coli glutamate-dependent acid resistance genes gadA and gadBC in an hns rpoS mutant
    • Waterman SR, Small PLC. 2003. Transcriptional expression of Escherichia coli glutamate-dependent acid resistance genes gadA and gadBC in an hns rpoS mutant. J Bacteriol 185:4644-4647.
    • (2003) J Bacteriol , vol.185 , pp. 4644-4647
    • Waterman, S.R.1    Small, P.L.C.2
  • 107
    • 0346964255 scopus 로고    scopus 로고
    • Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: antiactivation by the nucleoid proteins FIS and IHF
    • Browning DF, Beatty CM, Sanstad EA, Gunn KE, Busby SJW, Wolfe AJ. 2004. Modulation of CRP-dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: antiactivation by the nucleoid proteins FIS and IHF. Mol Microbiol 51:241-254.
    • (2004) Mol Microbiol , vol.51 , pp. 241-254
    • Browning, D.F.1    Beatty, C.M.2    Sanstad, E.A.3    Gunn, K.E.4    Busby, S.J.W.5    Wolfe, A.J.6
  • 108
    • 0031893742 scopus 로고    scopus 로고
    • Activation of Escherichia coli rRNA transcription by FIS during a growth cycle
    • Appleman JA, Ross W, Salomon J, Gourse RL. 1998. Activation of Escherichia coli rRNA transcription by FIS during a growth cycle. J Bacteriol 180:1525-1532.
    • (1998) J Bacteriol , vol.180 , pp. 1525-1532
    • Appleman, J.A.1    Ross, W.2    Salomon, J.3    Gourse, R.L.4
  • 109
    • 0037127209 scopus 로고    scopus 로고
    • Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1
    • Dame RT, Wyman C, Wurn R, Wagner R, Goosen N. 2002. Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1. J Biol Chem 277:2146-2150.
    • (2002) J Biol Chem , vol.277 , pp. 2146-2150
    • Dame, R.T.1    Wyman, C.2    Wurn, R.3    Wagner, R.4    Goosen, N.5
  • 110
    • 0023413823 scopus 로고
    • Cloning and sequencing of the HU-2 gene of Escherichia coli
    • Kano Y, Osato K, Wada M, Imamoto F. 1987. Cloning and sequencing of the HU-2 gene of Escherichia coli. Mol Gen Genet 209:408-410.
    • (1987) Mol Gen Genet , vol.209 , pp. 408-410
    • Kano, Y.1    Osato, K.2    Wada, M.3    Imamoto, F.4
  • 111
    • 0037823447 scopus 로고    scopus 로고
    • Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure
    • Ramstein J, Hervouet N, Coste F, Zelwer C, Oberto J, Castaing B. 2003. Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure. J Mol Biol 332:101-121.
    • (2003) J Mol Biol , vol.332 , pp. 101-121
    • Ramstein, J.1    Hervouet, N.2    Coste, F.3    Zelwer, C.4    Oberto, J.5    Castaing, B.6
  • 112
    • 1342324028 scopus 로고    scopus 로고
    • IHF and HU: flexible architects of bent DNA
    • Swinger KK, Rice PA. 2004. IHF and HU: flexible architects of bent DNA. Curr Opin Struct Biol 14:28-35.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 28-35
    • Swinger, K.K.1    Rice, P.A.2
  • 113
    • 0030601787 scopus 로고    scopus 로고
    • Regulation of HUa and HUβ by CRP and Fis in Escherichia col
    • Claret L, Rouviere-Yaniv J. 1996. Regulation of HUa and HUβ by CRP and Fis in Escherichia col. J Mol Biol 263:126-139.
    • (1996) J Mol Biol , vol.263 , pp. 126-139
    • Claret, L.1    Rouviere-Yaniv, J.2
  • 114
    • 0036231561 scopus 로고    scopus 로고
    • Selective expression of the nucleoid-associated protein HU during cold shock in Escherichia coli
    • Giangrossi M, Giuliodori AM, Gualerzi CO, Pon CL. 2002. Selective expression of the nucleoid-associated protein HU during cold shock in Escherichia coli. Mol Microbiol 44:206-216.
    • (2002) Mol Microbiol , vol.44 , pp. 206-216
    • Giangrossi, M.1    Giuliodori, A.M.2    Gualerzi, C.O.3    Pon, C.L.4
  • 115
    • 0034613020 scopus 로고    scopus 로고
    • Structural analysis of the transcription activation region on Fis: crystal structures of six Fis mutants with different activation properties
    • Cheng Y-S, Yang W-Z, Johnson RC, Yuan HS. 2000. Structural analysis of the transcription activation region on Fis: crystal structures of six Fis mutants with different activation properties. J Mol Biol 302:1139-1151.
    • (2000) J Mol Biol , vol.302 , pp. 1139-1151
    • Cheng, Y.-S.1    Yang, W.-Z.2    Johnson, R.C.3    Yuan, H.S.4
  • 118
  • 122
    • 0027172958 scopus 로고
    • Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli
    • Tanaka H, Goshima N, Kohno K, Kano Y, Imamoto F. 1993. Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli. J Biochem 113:568-572.
    • (1993) J Biochem , vol.113 , pp. 568-572
    • Tanaka, H.1    Goshima, N.2    Kohno, K.3    Kano, Y.4    Imamoto, F.5
  • 123
    • 0023041804 scopus 로고
    • Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosomelike structures with altered DNA helical pitch
    • Broyles SS, Pettijohn DE. 1986. Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosomelike structures with altered DNA helical pitch. J Mol Biol 187:47-60.
    • (1986) J Mol Biol , vol.187 , pp. 47-60
    • Broyles, S.S.1    Pettijohn, D.E.2
  • 124
    • 0028136642 scopus 로고
    • DNA binding parameters of the HU protein of Escherichia coli to cruciform DNA
    • Bonnefoy E, Takahashi M, Rouviere-Yaniv J. 1994. DNA binding parameters of the HU protein of Escherichia coli to cruciform DNA. J Mol Biol 242:116-129.
    • (1994) J Mol Biol , vol.242 , pp. 116-129
    • Bonnefoy, E.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 126
    • 33845796196 scopus 로고    scopus 로고
    • Structure-based analysis of HUDNA binding
    • Swinger KK, Rice PA. 2007. Structure-based analysis of HUDNA binding. J Mol Biol 365:1005-1016.
    • (2007) J Mol Biol , vol.365 , pp. 1005-1016
    • Swinger, K.K.1    Rice, P.A.2
  • 127
    • 28044436995 scopus 로고    scopus 로고
    • Nucleoid remodeling by an altered HU protein: Reorganization of the transcription program
    • Kar S, Edgar R, Adhya S. 2005. Nucleoid remodeling by an altered HU protein: Reorganization of the transcription program. Proc Natl Acad Sci USA 102:16397-16402.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16397-16402
    • Kar, S.1    Edgar, R.2    Adhya, S.3
  • 128
    • 19444387811 scopus 로고    scopus 로고
    • Bacterial repression loops requires enhanced DNA flexibility
    • Becker NA, Kahn JD, Maher LJ III. 2005. Bacterial repression loops requires enhanced DNA flexibility. J Mol Biol 349:716-730.
    • (2005) J Mol Biol , vol.349 , pp. 716-730
    • Becker, N.A.1    Kahn, J.D.2    Maher, L.J.3
  • 129
    • 0032945039 scopus 로고    scopus 로고
    • Role of HU and DNA supercoiling in transcription repression: specialized nucleoprotein repression complex at gal promoters in Escherichia coli
    • Lewis DE, Geanacopoulos M, Adhya S. 1999. Role of HU and DNA supercoiling in transcription repression: specialized nucleoprotein repression complex at gal promoters in Escherichia coli. Mol Microbiol 31:451-461.
    • (1999) Mol Microbiol , vol.31 , pp. 451-461
    • Lewis, D.E.1    Geanacopoulos, M.2    Adhya, S.3
  • 132
    • 0021346918 scopus 로고
    • Protein HU in the enzymatic replication of the chromosomal origin of Escherichia coli
    • Dixon NE, Kornberg A. 1984. Protein HU in the enzymatic replication of the chromosomal origin of Escherichia coli. Proc Natl Acad Sci USA 81:424-428.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 424-428
    • Dixon, N.E.1    Kornberg, A.2
  • 133
    • 0030908533 scopus 로고    scopus 로고
    • The Escherichia coli histonelike protein HU affects DNA initiation, chromosome partitioning via MukB, and cell division via MinCDE
    • Jaffe A, Vinella D, D'Ari R. 1997. The Escherichia coli histonelike protein HU affects DNA initiation, chromosome partitioning via MukB, and cell division via MinCDE. J Bacteriol 179:3494-3499.
    • (1997) J Bacteriol , vol.179 , pp. 3494-3499
    • Jaffe, A.1    Vinella, D.2    D'Ari, R.3
  • 134
    • 38449105269 scopus 로고    scopus 로고
    • Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin
    • Chodavarupu S, Felczak MM, Rouviere-Yaniv J, Kaguni JJ. 2008. Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin. Mol Microbiol 67:781-792.
    • (2008) Mol Microbiol , vol.67 , pp. 781-792
    • Chodavarupu, S.1    Felczak, M.M.2    Rouviere-Yaniv, J.3    Kaguni, J.J.4
  • 135
    • 0026325164 scopus 로고
    • Similarity between the DNAbinding domain of IHF protein and TFIID protein
    • Nash H, Granston AE. 1991. Similarity between the DNAbinding domain of IHF protein and TFIID protein. Cell 67:1037-1038.
    • (1991) Cell , vol.67 , pp. 1037-1038
    • Nash, H.1    Granston, A.E.2
  • 136
    • 41149097061 scopus 로고    scopus 로고
    • Mechanisms of specific and nonspecific binding of architectural proteins in prokaryotic gene regulation
    • Benevides JM, Danahy J, Kawakami J, Thomas GJ Jr. 2008. Mechanisms of specific and nonspecific binding of architectural proteins in prokaryotic gene regulation. Biochemistry 47:3855-3862.
    • (2008) Biochemistry , vol.47 , pp. 3855-3862
    • Benevides, J.M.1    Danahy, J.2    Kawakami, J.3    Thomas, G.J.4
  • 137
    • 33845504065 scopus 로고    scopus 로고
    • Direct observation of DNA bending/unbending kinetics in complex with DNA-bending protein IHF
    • Kuznetsov S, Sugimura S, Vivas P, Crothers DM, Snsari A. 2006. Direct observation of DNA bending/unbending kinetics in complex with DNA-bending protein IHF. Proc Natl Acad Sci USA 103:18515-18520.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18515-18520
    • Kuznetsov, S.1    Sugimura, S.2    Vivas, P.3    Crothers, D.M.4    Snsari, A.5
  • 138
    • 0024291348 scopus 로고
    • Integration host factor: a protein for all reasons
    • Friedman DI. 1988. Integration host factor: a protein for all reasons. Cell 55:545-554.
    • (1988) Cell , vol.55 , pp. 545-554
    • Friedman, D.I.1
  • 139
    • 0024463676 scopus 로고
    • Heteroduplex substrates for bacteriophage lambda site-specific recombination: cleavage and strand transfer products
    • Nash H, Robertson CA. 1989. Heteroduplex substrates for bacteriophage lambda site-specific recombination: cleavage and strand transfer products. EMBO J 8:3523-3933.
    • (1989) EMBO J , vol.8 , pp. 3523-3933
    • Nash, H.1    Robertson, C.A.2
  • 140
    • 0024340762 scopus 로고
    • DNA looping generated by DNA bending protein IHF and the two domains of lambda integrase
    • Vargas L, Kim S, Landy A. 1989. DNA looping generated by DNA bending protein IHF and the two domains of lambda integrase. Science 244:1457-1461.
    • (1989) Science , vol.244 , pp. 1457-1461
    • Vargas, L.1    Kim, S.2    Landy, A.3
  • 141
    • 0026705508 scopus 로고
    • The role of integration host factor in gene expression in Escherichia coli
    • Freundlich M, Ramani N, Mathew E, Sirko A, Tsui P. 1992. The role of integration host factor in gene expression in Escherichia coli. Mol Microbiol 6:2557-2563.
    • (1992) Mol Microbiol , vol.6 , pp. 2557-2563
    • Freundlich, M.1    Ramani, N.2    Mathew, E.3    Sirko, A.4    Tsui, P.5
  • 142
  • 144
    • 0033818258 scopus 로고    scopus 로고
    • Suppression of FNRdependent transcription activation at the Escherichia coli nir promoter by Fis, IHF and H-NS: modulation of transcription initiation by a complex nucleo-protein assembly
    • Browning DF, Cole JA, Busby SJW. 2000. Suppression of FNRdependent transcription activation at the Escherichia coli nir promoter by Fis, IHF and H-NS: modulation of transcription initiation by a complex nucleo-protein assembly. Mol Microbiol 37:1258-1269.
    • (2000) Mol Microbiol , vol.37 , pp. 1258-1269
    • Browning, D.F.1    Cole, J.A.2    Busby, S.J.W.3
  • 145
    • 33750445310 scopus 로고    scopus 로고
    • The Escherichia coli K-12 NarL and NarP proteins insulate the nrf promoter from the effects of integration host factor
    • Browning DF, Lee DJ, Wolfe AJ, Cole JA, Busby SJW. 2006. The Escherichia coli K-12 NarL and NarP proteins insulate the nrf promoter from the effects of integration host factor. J Bacteriol 188: 7449-7456.
    • (2006) J Bacteriol , vol.188 , pp. 7449-7456
    • Browning, D.F.1    Lee, D.J.2    Wolfe, A.J.3    Cole, J.A.4    Busby, S.J.W.5
  • 146
    • 0034973706 scopus 로고    scopus 로고
    • Activation from a distance: Roles of Lrp and integration host factor in transcription activation of gltBDF
    • Paul L, Blumenthal RM, Mathews RG. 2001. Activation from a distance: Roles of Lrp and integration host factor in transcription activation of gltBDF. J Bacteriol 183:3910-3918.
    • (2001) J Bacteriol , vol.183 , pp. 3910-3918
    • Paul, L.1    Blumenthal, R.M.2    Mathews, R.G.3
  • 147
    • 24944558886 scopus 로고    scopus 로고
    • Modulation of the sensitivity of FimB recombination to branched-chain amino acids and alanine in Escherichia coli K-12
    • Lahooti M, Roesch PL, Blomfield IC. 2005. Modulation of the sensitivity of FimB recombination to branched-chain amino acids and alanine in Escherichia coli K-12. J Bacteriol 187:6273-6280.
    • (2005) J Bacteriol , vol.187 , pp. 6273-6280
    • Lahooti, M.1    Roesch, P.L.2    Blomfield, I.C.3
  • 148
    • 33846597207 scopus 로고    scopus 로고
    • Multiple co-regulatory elements and IHF are necessary for the control of fimB expression in response to sialic acid and N-acetylglucosamine in Escherichia coli K-12
    • Sohanpal BK, Friar S, Roobol J, Plumbridge JA, Blomfield IC. 2007. Multiple co-regulatory elements and IHF are necessary for the control of fimB expression in response to sialic acid and N-acetylglucosamine in Escherichia coli K-12. Mol Microbiol 63:1223-1236.
    • (2007) Mol Microbiol , vol.63 , pp. 1223-1236
    • Sohanpal, B.K.1    Friar, S.2    Roobol, J.3    Plumbridge, J.A.4    Blomfield, I.C.5
  • 149
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • Altuvia S, Almiron M, Huissman G, Kolter R, Storz G. 1994. The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase. Mol Microbiol 13:265-272.
    • (1994) Mol Microbiol , vol.13 , pp. 265-272
    • Altuvia, S.1    Almiron, M.2    Huissman, G.3    Kolter, R.4    Storz, G.5
  • 150
    • 33644759551 scopus 로고    scopus 로고
    • The effect of IHF on sS selectivity of the phoA and pst promoters of Escherichia coli
    • Taschner NP, Yagil E, Spira B. 2006. The effect of IHF on sS selectivity of the phoA and pst promoters of Escherichia coli. Arch Microbiol 185:234-237.
    • (2006) Arch Microbiol , vol.185 , pp. 234-237
    • Taschner, N.P.1    Yagil, E.2    Spira, B.3
  • 151
    • 0028149835 scopus 로고
    • Expression of the genes coding for the Escherichia coli integration host factor are controlled by growth phase, rpoS, ppGpp and by autoregulation
    • Aviv M, Giladi H, Schreiber G, Oppenheim AB, Glaser G. 1994. Expression of the genes coding for the Escherichia coli integration host factor are controlled by growth phase, rpoS, ppGpp and by autoregulation. Mol Microbiol 14:1021-1031.
    • (1994) Mol Microbiol , vol.14 , pp. 1021-1031
    • Aviv, M.1    Giladi, H.2    Schreiber, G.3    Oppenheim, A.B.4    Glaser, G.5
  • 152
    • 0034660619 scopus 로고    scopus 로고
    • Sigma factor selectivity of Escherichia coli RNA polymerase: role for CRP, IHF and Lrp transcription factors
    • Colland F, Barth M, Hengge-Aronis R, Kolb A. 2006. Sigma factor selectivity of Escherichia coli RNA polymerase: role for CRP, IHF and Lrp transcription factors. EMBO J 19:3028-3037.
    • (2006) EMBO J , vol.19 , pp. 3028-3037
    • Colland, F.1    Barth, M.2    Hengge-Aronis, R.3    Kolb, A.4
  • 153
    • 0027941644 scopus 로고
    • Structure of the P22 att site: conservation and divergence in the motif of recombination complexes
    • Smith-Mungo L, Chan IT, Landy A. 1994. Structure of the P22 att site: conservation and divergence in the motif of recombination complexes. J Biol Chem 269:20798-20805.
    • (1994) J Biol Chem , vol.269 , pp. 20798-20805
    • Smith-Mungo, L.1    Chan, I.T.2    Landy, A.3
  • 154
    • 0011124187 scopus 로고    scopus 로고
    • Site-specific recombination of bacteriophage P22 does not require integration host factor
    • Cho EH, Num C-E, Alcaraz R Jr, Gardner JF. 1999. Site-specific recombination of bacteriophage P22 does not require integration host factor. J Bacteriol 181:4245-4249.
    • (1999) J Bacteriol , vol.181 , pp. 4245-4249
    • Cho, E.H.1    Num, C.-E.2    Alcaraz, R.3    Gardner, J.F.4
  • 155
    • 0029952986 scopus 로고    scopus 로고
    • In vitro transcriptional analysis of TyrR-mediated activation of the mtr and tyrP+3 promotes of Escherichia coli
    • Yang J, Camakaris H, Pittard AJ. 1996. In vitro transcriptional analysis of TyrR-mediated activation of the mtr and tyrP+3 promotes of Escherichia coli. J Bacteriol 178:6389-6393.
    • (1996) J Bacteriol , vol.178 , pp. 6389-6393
    • Yang, J.1    Camakaris, H.2    Pittard, A.J.3
  • 156
    • 0026031442 scopus 로고
    • HU nd integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by erminase
    • Mendelson I, Gottesman M, Oppenheim AB. 1991. HU nd integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by erminase. J Bacteriol 173:1670-1676.
    • (1991) J Bacteriol , vol.173 , pp. 1670-1676
    • Mendelson, I.1    Gottesman, M.2    Oppenheim, A.B.3
  • 157
  • 158
    • 0021760528 scopus 로고
    • Hla, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro
    • Spassky A, Rimsky S, Garreau H, Buc H. 1984. Hla, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro. Nucleic Acids Res 12:5321-5340.
    • (1984) Nucleic Acids Res , vol.12 , pp. 5321-5340
    • Spassky, A.1    Rimsky, S.2    Garreau, H.3    Buc, H.4
  • 160
    • 0242289416 scopus 로고    scopus 로고
    • H-NS in gram-negative bacteria: a family of multifaceted proteins
    • Tendeng G, Bertin PN. 2003. H-NS in gram-negative bacteria: a family of multifaceted proteins. Trends Microbiol 11:511-518.
    • (2003) Trends Microbiol , vol.11 , pp. 511-518
    • Tendeng, G.1    Bertin, P.N.2
  • 163
    • 0024004997 scopus 로고
    • Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 14-kD Escherichia coli DNA binding protein H-NS
    • Falconi M, Gualtieri MT, La Teana A, Losso MA, Pon CL. 1988. Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 14-kD Escherichia coli DNA binding protein H-NS. Mol Microbiol 2:323-329.
    • (1988) Mol Microbiol , vol.2 , pp. 323-329
    • Falconi, M.1    Gualtieri, M.T.2    La Teana, A.3    Losso, M.A.4    Pon, C.L.5
  • 164
    • 0033970889 scopus 로고    scopus 로고
    • Multimeric self-assembly equilibrium involving the histonelike protein H-NS. A thermodynamic study
    • Ceschini S, Lupidi G, Coletta M, Pon CL, Fioretti E, Angeletti M. 2000. Multimeric self-assembly equilibrium involving the histonelike protein H-NS. A thermodynamic study. J Biol Chem 275:729-734.
    • (2000) J Biol Chem , vol.275 , pp. 729-734
    • Ceschini, S.1    Lupidi, G.2    Coletta, M.3    Pon, C.L.4    Fioretti, E.5    Angeletti, M.6
  • 165
    • 0027073133 scopus 로고
    • Nucleotide sequence of a newlyidentified Escherichia gene, stpA, encoding an H-NS-like protein
    • Zhang A, Belfort M. 1992. Nucleotide sequence of a newlyidentified Escherichia gene, stpA, encoding an H-NS-like protein. Nucleic Acids Res 20:6735.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6735
    • Zhang, A.1    Belfort, M.2
  • 166
    • 0035078382 scopus 로고    scopus 로고
    • Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli
    • Johnson J, Eriksson S, Sonden B, Wai SN, Uhlin BE. 2001. Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli. J Bacteriol 183:2343-2347.
    • (2001) J Bacteriol , vol.183 , pp. 2343-2347
    • Johnson, J.1    Eriksson, S.2    Sonden, B.3    Wai, S.N.4    Uhlin, B.E.5
  • 167
    • 0029785418 scopus 로고    scopus 로고
    • Probing the structure, function and interactions of the Escherichia coli H-NS and StpA proteins using dominant negative derivatives
    • Williams RM, Rimsky S, Buc H. 1996. Probing the structure, function and interactions of the Escherichia coli H-NS and StpA proteins using dominant negative derivatives. J Bacteriol 178:4335-4343.
    • (1996) J Bacteriol , vol.178 , pp. 4335-4343
    • Williams, R.M.1    Rimsky, S.2    Buc, H.3
  • 170
    • 0036174055 scopus 로고    scopus 로고
    • Evidence for direct protein-protein interaction between members of the enterobacterial HhaA/YmoA and H-NS families of proteins
    • Nieto JM, Madrid C, Miquelay E, Parra JL, Rodriguez S, Juarez A. 2002. Evidence for direct protein-protein interaction between members of the enterobacterial HhaA/YmoA and H-NS families of proteins. J Bacteriol 184:629-635.
    • (2002) J Bacteriol , vol.184 , pp. 629-635
    • Nieto, J.M.1    Madrid, C.2    Miquelay, E.3    Parra, J.L.4    Rodriguez, S.5    Juarez, A.6
  • 171
    • 39649101686 scopus 로고    scopus 로고
    • Structure of the nucleoid-associated protein Cnu reveals common binding sites for HNS in Cnu and Hha
    • Bae SH, Liu D, Lim HM, Lee Y, Choi BS. 2008. Structure of the nucleoid-associated protein Cnu reveals common binding sites for HNS in Cnu and Hha. Biochemistry 47:1993-2001.
    • (2008) Biochemistry , vol.47 , pp. 1993-2001
    • Bae, S.H.1    Liu, D.2    Lim, H.M.3    Lee, Y.4    Choi, B.S.5
  • 172
    • 0032825041 scopus 로고    scopus 로고
    • Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary phase survival of Escherichia coli
    • Johansson J, Uhlin BE. 1999. Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary phase survival of Escherichia coli. Proc Natl Acad Sci USA 96:10776-10781.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10776-10781
    • Johansson, J.1    Uhlin, B.E.2
  • 173
    • 0036723747 scopus 로고    scopus 로고
    • Temperature-and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin
    • Madrid C, Nieto JM, Paytubi S, Falconi F, Guralerzi CO, Juarez A. 2002. Temperature-and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin. J Bacteriol 184:5058-5066.
    • (2002) J Bacteriol , vol.184 , pp. 5058-5066
    • Madrid, C.1    Nieto, J.M.2    Paytubi, S.3    Falconi, F.4    Guralerzi, C.O.5    Juarez, A.6
  • 174
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun X, Zhulin I, Watell RM. 2002. Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res 30:3662-3671.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3662-3671
    • Sun, X.1    Zhulin, I.2    Watell, R.M.3
  • 175
    • 2442483884 scopus 로고    scopus 로고
    • The DNA binding protein H-NS binds to and alters the stability of RNA in vitro and in vivo
    • Brescia CC, Kaw MK, Sledjeski DD. 2004. The DNA binding protein H-NS binds to and alters the stability of RNA in vitro and in vivo. J Mol Biol 339:505-514.
    • (2004) J Mol Biol , vol.339 , pp. 505-514
    • Brescia, C.C.1    Kaw, M.K.2    Sledjeski, D.D.3
  • 176
    • 0037367939 scopus 로고    scopus 로고
    • RNA chaperone activity of the Sm-like Hfq protein
    • Moll I, Leitsch D, Steinhauser T, Blaesi U. 2003. RNA chaperone activity of the Sm-like Hfq protein. EMBO Rep 4:284-289.
    • (2003) EMBO Rep , vol.4 , pp. 284-289
    • Moll, I.1    Leitsch, D.2    Steinhauser, T.3    Blaesi, U.4
  • 177
    • 0029913710 scopus 로고    scopus 로고
    • Escherichia coli protein analogs StpA and H-NS regulatory loops, similar and disparate effects on nucleic acid dynamics
    • Zhang A, Rimsky S, Reaban ME, Buc H, Belfort M. 1996. Escherichia coli protein analogs StpA and H-NS regulatory loops, similar and disparate effects on nucleic acid dynamics. EMBO J 15:1340-1349.
    • (1996) EMBO J , vol.15 , pp. 1340-1349
    • Zhang, A.1    Rimsky, S.2    Reaban, M.E.3    Buc, H.4    Belfort, M.5
  • 178
    • 0024828668 scopus 로고
    • Synthetic curved DNA sequences can act as transcriptional activators in Escherichia coli
    • Bracco L, Kotlarg D, A Kolb, Diekmann S, Buc H. 1989. Synthetic curved DNA sequences can act as transcriptional activators in Escherichia coli. EMBO J 8:4289-4296.
    • (1989) EMBO J , vol.8 , pp. 4289-4296
    • Bracco, L.1    Kotlarg, D.2    Kolb, A.3    Diekmann, S.4    Buc, H.5
  • 179
    • 0035083490 scopus 로고    scopus 로고
    • Structural basis for preferential binding of H-NS to curved DNA
    • Dame RT, Wyman C, Goosen N. 2001. Structural basis for preferential binding of H-NS to curved DNA. Biochimie 83:231-234.
    • (2001) Biochimie , vol.83 , pp. 231-234
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 181
    • 0035725521 scopus 로고    scopus 로고
    • A molecular mechanism for the repression of transcription by the H-NS protein
    • Rimsky S, Zuber F, Buckle M, Buc H. 2001. A molecular mechanism for the repression of transcription by the H-NS protein. Mol Microbiol 45:1311-1323.
    • (2001) Mol Microbiol , vol.45 , pp. 1311-1323
    • Rimsky, S.1    Zuber, F.2    Buckle, M.3    Buc, H.4
  • 182
    • 0025003429 scopus 로고
    • An Escherichia coli protein that preferentially binds to sharply curved DNA
    • Yamada H, Muramatsu S, Mizuno T. 1990. An Escherichia coli protein that preferentially binds to sharply curved DNA. J Biochem 108:420-425.
    • (1990) J Biochem , vol.108 , pp. 420-425
    • Yamada, H.1    Muramatsu, S.2    Mizuno, T.3
  • 184
    • 33750898424 scopus 로고    scopus 로고
    • Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase
    • Oshima T, Ishikawa S, Kurokawa K, Aiba H, Ogasawara N. 2006. Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase. DNA Res 13:141-153.
    • (2006) DNA Res , vol.13 , pp. 141-153
    • Oshima, T.1    Ishikawa, S.2    Kurokawa, K.3    Aiba, H.4    Ogasawara, N.5
  • 185
    • 0037381991 scopus 로고    scopus 로고
    • Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor
    • Amit R, Oppenheim AB, Stavans J. 2003. Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor. Biophys J 84:2467-2473.
    • (2003) Biophys J , vol.84 , pp. 2467-2473
    • Amit, R.1    Oppenheim, A.B.2    Stavans, J.3
  • 189
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame RT, Wyman C, Goosen N. 2000. H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res 28:3504-3510.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 190
    • 0026573628 scopus 로고
    • Lethal overproduction of the Escherichia coli nucleoid protein H-NS: ultramicroscopic and molecular autopsy
    • Spurio R, Duttenberger M, Falconi M, La Teana A, Pon CL, Gualerzi CO. 1992. Lethal overproduction of the Escherichia coli nucleoid protein H-NS: ultramicroscopic and molecular autopsy. Mol Gen Genet 231:201-211.
    • (1992) Mol Gen Genet , vol.231 , pp. 201-211
    • Spurio, R.1    Duttenberger, M.2    Falconi, M.3    La Teana, A.4    Pon, C.L.5    Gualerzi, C.O.6
  • 191
    • 0030977555 scopus 로고    scopus 로고
    • In vivo supercoiling of plasmid and chromosomal DNA in an Escherichia coli hns mutant
    • Mojica FJ, Higgins CF. 1997. In vivo supercoiling of plasmid and chromosomal DNA in an Escherichia coli hns mutant. J Bacteriol 179:3528-3533.
    • (1997) J Bacteriol , vol.179 , pp. 3528-3533
    • Mojica, F.J.1    Higgins, C.F.2
  • 193
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: a universal regulator for a dynamic genome
    • Dorman C. 2004. H-NS: a universal regulator for a dynamic genome. Nat Rev Microbiol 2:391-400.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 391-400
    • Dorman, C.1
  • 195
    • 0027408394 scopus 로고
    • The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor
    • Ueguchi C, Mizuno T. 1993. The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor. EMBO J 12:1039-1046.
    • (1993) EMBO J , vol.12 , pp. 1039-1046
    • Ueguchi, C.1    Mizuno, T.2
  • 196
    • 20444417420 scopus 로고    scopus 로고
    • Antagonistic role of H-NS and GadX in the regulation of the glutamate decarboxylase-dependent acid resistance system in Escherichia coli
    • Giangrossi M, Zattoni S, Tramonti A, de Biase D, Falconi M. 2005. Antagonistic role of H-NS and GadX in the regulation of the glutamate decarboxylase-dependent acid resistance system in Escherichia coli. J Biol Chem 280:21498-21505.
    • (2005) J Biol Chem , vol.280 , pp. 21498-21505
    • Giangrossi, M.1    Zattoni, S.2    Tramonti, A.3    de Biase, D.4    Falconi, M.5
  • 197
    • 14244252782 scopus 로고    scopus 로고
    • A cis-spreading nucleoprotein filament is responsible for the gene silencing activity found in the promoter relay mechanism
    • Chen C-C, Chou M-Y, Huang C-H, Majumder A, Wu H-Y. 2005. A cis-spreading nucleoprotein filament is responsible for the gene silencing activity found in the promoter relay mechanism. J Biol Chem 280:5101-5112.
    • (2005) J Biol Chem , vol.280 , pp. 5101-5112
    • Chen, C.-C.1    Chou, M.-Y.2    Huang, C.-H.3    Majumder, A.4    Wu, H.-Y.5
  • 198
    • 34247628510 scopus 로고    scopus 로고
    • H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing
    • Bouffartigues E, Buckle M, Badaut C, Travers A, Rimsky S. 2007. H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing. Nat Struct Mol Biol 14: 441-448.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 441-448
    • Bouffartigues, E.1    Buckle, M.2    Badaut, C.3    Travers, A.4    Rimsky, S.5
  • 199
    • 84959092031 scopus 로고    scopus 로고
    • Lac and lambda repressors relieve silencing of the Escherichia coli bgl promoter: activation by alternation of a repressing nucleoprotein complex
    • Caremel AM, Schnetz J. 1998. Lac and lambda repressors relieve silencing of the Escherichia coli bgl promoter: activation by alternation of a repressing nucleoprotein complex. J Mol Biol 42:439-452.
    • (1998) J Mol Biol , vol.42 , pp. 439-452
    • Caremel, A.M.1    Schnetz, J.2
  • 200
    • 0034767928 scopus 로고    scopus 로고
    • Involvement of Fis in the H-NS-mediated regulation of virF gene of Shigella and enteroinvasive Escherichia coli
    • Falconi M, Prosseda G, Giangrossi M, Beghetto E, Colonna B. 2001. Involvement of Fis in the H-NS-mediated regulation of virF gene of Shigella and enteroinvasive Escherichia coli. Mol Microbiol 42:439-452.
    • (2001) Mol Microbiol , vol.42 , pp. 439-452
    • Falconi, M.1    Prosseda, G.2    Giangrossi, M.3    Beghetto, E.4    Colonna, B.5
  • 201
    • 0026776718 scopus 로고
    • The positive regulator CfaD overcomes the repression mediated by histone-like protein H-NS (H1) in the CFA/1 fimbrial operon of Escherichia coli
    • Jordi B, Dagberg B, de Haan LA, Hamers AM, van der Zeijst BA, Gaastra W, Uhlin BE. 1992. The positive regulator CfaD overcomes the repression mediated by histone-like protein H-NS (H1) in the CFA/1 fimbrial operon of Escherichia coli. EMBO J 11:2627-2632.
    • (1992) EMBO J , vol.11 , pp. 2627-2632
    • Jordi, B.1    Dagberg, B.2    de Haan, L.A.3    Hamers, A.M.4    van der Zeijst, B.A.5    Gaastra, W.6    Uhlin, B.E.7
  • 203
    • 33846637687 scopus 로고    scopus 로고
    • The role of LRP and H-NS in transcription regulation: involvement of synergism, allostery and macromolecular crowding
    • Pul U, Wurm R, Wagner R. 2007. The role of LRP and H-NS in transcription regulation: involvement of synergism, allostery and macromolecular crowding. J Mol Biol 336:900-915.
    • (2007) J Mol Biol , vol.336 , pp. 900-915
    • Pul, U.1    Wurm, R.2    Wagner, R.3
  • 205
    • 33746629034 scopus 로고    scopus 로고
    • Role of histone-like proteins H-NS and StpA in expression of virulence determinants of uropathogenic Escherichia coli
    • Muller CM, Dobrindt U, Nagy G, Emody L, Uhlin BE, Hacker J. 2006. Role of histone-like proteins H-NS and StpA in expression of virulence determinants of uropathogenic Escherichia coli. J Bacteriol 188:5426-5438.
    • (2006) J Bacteriol , vol.188 , pp. 5426-5438
    • Muller, C.M.1    Dobrindt, U.2    Nagy, G.3    Emody, L.4    Uhlin, B.E.5    Hacker, J.6
  • 206
    • 36348945338 scopus 로고    scopus 로고
    • SlyA and H-NS regulate transcription of slyA in Escherichia coli is temperature-dependent, positively autoregulated, and independent of H-NS
    • Corbett D, Bennett HJ, Askar H, Green J, Roberts S. 2007. SlyA and H-NS regulate transcription of slyA in Escherichia coli is temperature-dependent, positively autoregulated, and independent of H-NS. J Biol Chem 282:33326-33335.
    • (2007) J Biol Chem , vol.282 , pp. 33326-33335
    • Corbett, D.1    Bennett, H.J.2    Askar, H.3    Green, J.4    Roberts, S.5
  • 207
    • 35448991375 scopus 로고    scopus 로고
    • Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12
    • Lithgow JK, Haider F, Roberts IS, Green J. 2007. Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12. Mol Microbiol 66:685-698.
    • (2007) Mol Microbiol , vol.66 , pp. 685-698
    • Lithgow, J.K.1    Haider, F.2    Roberts, I.S.3    Green, J.4
  • 208
    • 0036280133 scopus 로고    scopus 로고
    • Differential regulation of multiple proteins of Escherichia coli and Salmonella enterica serovar Typhimurium by the transcriptional regulator SlyA
    • Spory A, BosserhoffA, von Rhein C, Goebel W, Ludwig A. 2002. Differential regulation of multiple proteins of Escherichia coli and Salmonella enterica serovar Typhimurium by the transcriptional regulator SlyA. J Bacteriol 184:3549-3559.
    • (2002) J Bacteriol , vol.184 , pp. 3549-3559
    • Spory, A.1    Bosserhoff, A.2    von Rhein, C.3    Goebel, W.4    Ludwig, A.5
  • 209
    • 33846465923 scopus 로고    scopus 로고
    • H-NS, the genome sentinel
    • Dorman C. 2007. H-NS, the genome sentinel. Nat Rev Microbiol 5:157-161.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 157-161
    • Dorman, C.1
  • 210
    • 63449108030 scopus 로고    scopus 로고
    • Genome-wide identification of H-NS-controlled, temperature-regulated genes in Escherichia coli K-12
    • White-Ziegler CA, Davis TR. 2009. Genome-wide identification of H-NS-controlled, temperature-regulated genes in Escherichia coli K-12. J Bacteriol 191:1106-1110.
    • (2009) J Bacteriol , vol.191 , pp. 1106-1110
    • White-Ziegler, C.A.1    Davis, T.R.2
  • 211
    • 0034682744 scopus 로고    scopus 로고
    • Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli
    • Johansson J, Balsalobre C, Wang S-Y, Urbonaviciene J, Jin DJ, Sonden B, Uhlin BE. 2000. Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli. Cell 102:475-485.
    • (2000) Cell , vol.102 , pp. 475-485
    • Johansson, J.1    Balsalobre, C.2    Wang, S.-Y.3    Urbonaviciene, J.4    Jin, D.J.5    Sonden, B.6    Uhlin, B.E.7
  • 212
    • 0032796421 scopus 로고    scopus 로고
    • Multiple control of flagellum biosynthesis in Escherichia coli: Role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon
    • Soutourina O, Kolb A, Krin E, Laurent-Winter C, Rimsky S, Danchin A, Bertin P. 1999. Multiple control of flagellum biosynthesis in Escherichia coli: Role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon. J Bacteriol 181:7500-7508.
    • (1999) J Bacteriol , vol.181 , pp. 7500-7508
    • Soutourina, O.1    Kolb, A.2    Krin, E.3    Laurent-Winter, C.4    Rimsky, S.5    Danchin, A.6    Bertin, P.7
  • 213
    • 0034721950 scopus 로고    scopus 로고
    • Two novel flagella components and H-NS are involved in the motor function of Escherichia coli
    • Ko M, Park C. 2000. Two novel flagella components and H-NS are involved in the motor function of Escherichia coli. J Mol Biol 303:371-382.
    • (2000) J Mol Biol , vol.303 , pp. 371-382
    • Ko, M.1    Park, C.2
  • 214
    • 0026661849 scopus 로고
    • Expression and mutational analysis of the nucleoid-associated protein H-NS in Salmonella typhimurium
    • Hinton JC, D, Santos DS, SeirafiA, Hulton CS, Pavitt GD, Higgins CF. 1992. Expression and mutational analysis of the nucleoid-associated protein H-NS in Salmonella typhimurium. Mol Microbiol 6:2327-2337.
    • (1992) Mol Microbiol , vol.6 , pp. 2327-2337
    • Hinton, J.C.D.1    Santos, D.S.2    Seirafi, A.3    Hulton, C.S.4    Pavitt, G.D.5    Higgins, C.F.6
  • 215
    • 0025790144 scopus 로고
    • Identification of a cold shock transcription enhancer of the Escherichia coli gene encoding nucleoid protein H-NS
    • La Teana A, Brandi A, Falconi M, Spurio R, Pon CL, Galerzi CO. 1991. Identification of a cold shock transcription enhancer of the Escherichia coli gene encoding nucleoid protein H-NS. Proc Natl Acad Sci USA 88:10907-10911.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10907-10911
    • La Teana, A.1    Brandi, A.2    Falconi, M.3    Spurio, R.4    Pon, C.L.5    Galerzi, C.O.6
  • 216
    • 0027370350 scopus 로고
    • Stress response of Escherichia coli at elevated hydrostatic pressure
    • Welch TJ, Farewell A, Neidhardt FC, Bartlett DH. 1993. Stress response of Escherichia coli at elevated hydrostatic pressure. J Bacteriol 175:7170-7177.
    • (1993) J Bacteriol , vol.175 , pp. 7170-7177
    • Welch, T.J.1    Farewell, A.2    Neidhardt, F.C.3    Bartlett, D.H.4
  • 217
    • 0025939520 scopus 로고
    • The molecular structure of wildtype and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding
    • Yuan HS, Finkel SE, Feng JA, Kaczor-Grzeskowiiak M, Johnson RC, Dickerson RE. 1991. The molecular structure of wildtype and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding. Proc Natl Acad Sci USA 88:9556-9562.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9556-9562
    • Yuan, H.S.1    Finkel, S.E.2    Feng, J.A.3    Kaczor-Grzeskowiiak, M.4    Johnson, R.C.5    Dickerson, R.E.6
  • 218
    • 0024596904 scopus 로고
    • Bent DNA is needed for recombinational enhancer activity in the site-specific recombination system cin of bacteriophage P1: the role of Fis protein
    • Hubner P, Haffter P, Iida S, Arber W. 1989. Bent DNA is needed for recombinational enhancer activity in the site-specific recombination system cin of bacteriophage P1: the role of Fis protein. J Mol Biol 205:493-500.
    • (1989) J Mol Biol , vol.205 , pp. 493-500
    • Hubner, P.1    Haffter, P.2    Iida, S.3    Arber, W.4
  • 220
    • 44949157717 scopus 로고    scopus 로고
    • Biochemical identification of base and phosphate contacts between Fis and a highaffinity DNA binding site
    • Shao Y, Feldman-Cohen LS, Osuna R. 2008. Biochemical identification of base and phosphate contacts between Fis and a highaffinity DNA binding site. J Mol Biol 380:327-339.
    • (2008) J Mol Biol , vol.380 , pp. 327-339
    • Shao, Y.1    Feldman-Cohen, L.S.2    Osuna, R.3
  • 221
    • 44849093465 scopus 로고    scopus 로고
    • Genomewide analysis of Fis binding in Escherichia coli indicates a causative role for A-A/T-tracts
    • Cho BK, Knight EM, Barrett CL, Palsson BO. 2008. Genomewide analysis of Fis binding in Escherichia coli indicates a causative role for A-A/T-tracts. Genome Res 18:900-910.
    • (2008) Genome Res , vol.18 , pp. 900-910
    • Cho, B.K.1    Knight, E.M.2    Barrett, C.L.3    Palsson, B.O.4
  • 223
    • 19244372639 scopus 로고    scopus 로고
    • Variable structures of FIS-DNA complexes determined by flanking DNA-protein contacts
    • Pan CQ, Finkel SE, Cramton SE, Feng J, Sigman DS, Johnson RC. 1996. Variable structures of FIS-DNA complexes determined by flanking DNA-protein contacts. J Mol Biol 264:675-695.
    • (1996) J Mol Biol , vol.264 , pp. 675-695
    • Pan, C.Q.1    Finkel, S.E.2    Cramton, S.E.3    Feng, J.4    Sigman, D.S.5    Johnson, R.C.6
  • 224
    • 1842557558 scopus 로고    scopus 로고
    • Transcription activation by remodeling of a nucleoprotein assembly: the role of NarL at the FNR-dependent Escherichia coli nir promoter
    • Browning DF, Cole JA, Busby SJW. 2004. Transcription activation by remodeling of a nucleoprotein assembly: the role of NarL at the FNR-dependent Escherichia coli nir promoter. Mol Microbiol 53: 203-215.
    • (2004) Mol Microbiol , vol.53 , pp. 203-215
    • Browning, D.F.1    Cole, J.A.2    Busby, S.J.W.3
  • 225
    • 48449107161 scopus 로고    scopus 로고
    • Downregulation of the Escherichia coli guaB promoter by FIS
    • Husnain SI, Thomas MS. 2008. Downregulation of the Escherichia coli guaB promoter by FIS. Microbiology 154:1729-1738.
    • (2008) Microbiology , vol.154 , pp. 1729-1738
    • Husnain, S.I.1    Thomas, M.S.2
  • 227
    • 0025069971 scopus 로고
    • The role of Fis in transcription activation of stable RNA operons
    • Nilsson LA, Vanet A, Vijgenboom E, Bosch L. 1990. The role of Fis in transcription activation of stable RNA operons. EMBO J 9:727-737.
    • (1990) EMBO J , vol.9 , pp. 727-737
    • Nilsson, L.A.1    Vanet, A.2    Vijgenboom, E.3    Bosch, L.4
  • 228
    • 0025163439 scopus 로고
    • E. coli Fis protein activates rRNA transcription in vitro and in vivo
    • Ross W, Thompson JF, Newlands JT, Gourse RL. 1990. E. coli Fis protein activates rRNA transcription in vitro and in vivo. EMBO J 9:3733-3742.
    • (1990) EMBO J , vol.9 , pp. 3733-3742
    • Ross, W.1    Thompson, J.F.2    Newlands, J.T.3    Gourse, R.L.4
  • 229
    • 0029813128 scopus 로고    scopus 로고
    • A positive control mutant of the transcription activator protein FIS
    • Gosink KK, Gaal T, Bokal AJ IV, Goourse RL. 1996. A positive control mutant of the transcription activator protein FIS. J Bacteriol 178:5182-5187.
    • (1996) J Bacteriol , vol.178 , pp. 5182-5187
    • Gosink, K.K.1    Gaal, T.2    Bokal, A.J.3    Goourse, R.L.4
  • 230
    • 33748047157 scopus 로고    scopus 로고
    • RNA polymerase and an activator form discrete subcomplexes in a transcription initiation complex
    • Maurer S, Fritz J, Muskhelishvili G, Travers. 2006. RNA polymerase and an activator form discrete subcomplexes in a transcription initiation complex. EMBO J 25:3784-3790.
    • (2006) EMBO J , vol.25 , pp. 3784-3790
    • Maurer, S.1    Fritz, J.2    Muskhelishvili, G.3    Travers4
  • 233
    • 0028816422 scopus 로고
    • Identification of genes negatively regulated by Fis: Fis and RpoS comodulate growth-phase-dependent gene expression in Escherichia coli
    • Xu J, Johnson RC. 1995. Identification of genes negatively regulated by Fis: Fis and RpoS comodulate growth-phase-dependent gene expression in Escherichia coli. J Bacteriol 177:938-947.
    • (1995) J Bacteriol , vol.177 , pp. 938-947
    • Xu, J.1    Johnson, R.C.2
  • 234
    • 0345730808 scopus 로고    scopus 로고
    • Growth phase-dependent regulation and stringent control of fis are conserved processes in enteric bacteria and involve a single promoter (fisP) in Escherichia coli
    • Mallik P, Pratt TS, Beach MB, Bradley MD, Undamatla J, Osuna R. 2004. Growth phase-dependent regulation and stringent control of fis are conserved processes in enteric bacteria and involve a single promoter (fisP) in Escherichia coli. J Bacteriol 186:122-135.
    • (2004) J Bacteriol , vol.186 , pp. 122-135
    • Mallik, P.1    Pratt, T.S.2    Beach, M.B.3    Bradley, M.D.4    Undamatla, J.5    Osuna, R.6
  • 235
    • 0035947613 scopus 로고    scopus 로고
    • CRP modulates fis transcription by alternate formation of activating and repressing nucleoprotein complexes
    • Nasser W, Schneider R, Travers A, Muskhelishvili G. 2001. CRP modulates fis transcription by alternate formation of activating and repressing nucleoprotein complexes. J Biol Chem 275:17878-17886.
    • (2001) J Biol Chem , vol.275 , pp. 17878-17886
    • Nasser, W.1    Schneider, R.2    Travers, A.3    Muskhelishvili, G.4
  • 236
    • 0031733414 scopus 로고    scopus 로고
    • Identification and characterization of the fis operon in enteric bacteria
    • Beach MB, Osuna R. 1998. Identification and characterization of the fis operon in enteric bacteria. J Bacteriol 180:5932-5946.
    • (1998) J Bacteriol , vol.180 , pp. 5932-5946
    • Beach, M.B.1    Osuna, R.2
  • 237
    • 0026569267 scopus 로고
    • The E. coli fis promoter is subject to stringent control and autoregulation
    • Ninneman O, Koch C, Kahmann R. 1992. The E. coli fis promoter is subject to stringent control and autoregulation. EMBO J 11: 1075-1083.
    • (1992) EMBO J , vol.11 , pp. 1075-1083
    • Ninneman, O.1    Koch, C.2    Kahmann, R.3
  • 238
    • 0033063805 scopus 로고    scopus 로고
    • Functional determinants of the Escherichia coli fis promoter: roles of-35,-10, and transcription initiation regions in the response to stringent control and growth phase-dependent regulation
    • Walker KA, Atkins CL, Osuna R. 1999. Functional determinants of the Escherichia coli fis promoter: roles of-35,-10, and transcription initiation regions in the response to stringent control and growth phase-dependent regulation. J Bacteriol 181:1269-1280.
    • (1999) J Bacteriol , vol.181 , pp. 1269-1280
    • Walker, K.A.1    Atkins, C.L.2    Osuna, R.3
  • 239
    • 10944232640 scopus 로고    scopus 로고
    • The Escherichia coli fis promoter is regulated by changes in the levels of its transcription initiation nucleotide CTP
    • Walker KA, Malik P, Pratt TS, Osuna R. 2004. The Escherichia coli fis promoter is regulated by changes in the levels of its transcription initiation nucleotide CTP. J Biol Chem 279:50818-50828.
    • (2004) J Biol Chem , vol.279 , pp. 50818-50828
    • Walker, K.A.1    Malik, P.2    Pratt, T.S.3    Osuna, R.4
  • 241
    • 0031919615 scopus 로고    scopus 로고
    • BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells
    • Farris M, Grant A, Richardson TB, O'Connor CD. 1998. BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells. Mol Microbiol 28:265-279.
    • (1998) Mol Microbiol , vol.28 , pp. 265-279
    • Farris, M.1    Grant, A.2    Richardson, T.B.3    O'Connor, C.D.4
  • 242
    • 0027083350 scopus 로고
    • A novel DNAbinding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron M, Link AJ, Furlog D, Kolter R. 1992. A novel DNAbinding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6:2624-2654.
    • (1992) Genes Dev , vol.6 , pp. 2624-2654
    • Almiron, M.1    Link, A.J.2    Furlog, D.3    Kolter, R.4
  • 243
    • 44249126516 scopus 로고    scopus 로고
    • Selective repression by Fis and H-NS at the Escherichia coli dps promoter
    • Grainger DC, Goldberg MD, Lee DJ, Busby SJ. 2008. Selective repression by Fis and H-NS at the Escherichia coli dps promoter. Mol Microbiol 68:1366-1377.
    • (2008) Mol Microbiol , vol.68 , pp. 1366-1377
    • Grainger, D.C.1    Goldberg, M.D.2    Lee, D.J.3    Busby, S.J.4
  • 244
    • 44249112381 scopus 로고    scopus 로고
    • Fine-tuned growth phase control of dps, encoding a DNA protection protein, by FIS and H-NS
    • Schnetz K. 2008. Fine-tuned growth phase control of dps, encoding a DNA protection protein, by FIS and H-NS. Mol Microbiol 68:1345-1347.
    • (2008) Mol Microbiol , vol.68 , pp. 1345-1347
    • Schnetz, K.1
  • 245
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • Ren B, Tibbelin G, Kajino T, Asami O, Ladenstein R. 2003. The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. J Mol Biol 329:467-477.
    • (2003) J Mol Biol , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 246
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • Ceci P, Cellai S, Falvo E, Rivetti C, Rossi GL, Chiancone E. 2004. DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus. Nucleic Acids Res 32:5935-5944.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 247
    • 0141566368 scopus 로고    scopus 로고
    • Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli
    • Stephani K, Weichart D, Hengge R. 2003. Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Mol Microbiol 49:1605-1614.
    • (2003) Mol Microbiol , vol.49 , pp. 1605-1614
    • Stephani, K.1    Weichart, D.2    Hengge, R.3
  • 248
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the non-specific DNA-binding protein Dps
    • Martinez A, Kolter R. 1997. Protection of DNA during oxidative stress by the non-specific DNA-binding protein Dps. J Bacteriol 179: 5188-5194.
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 249
    • 0037020069 scopus 로고    scopus 로고
    • Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core
    • Ilari A, Ceci P, Ferrari D, Rossi GL, Chiancone C. 2002. Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J Biol Chem 277:37619-37623.
    • (2002) J Biol Chem , vol.277 , pp. 37619-37623
    • Ilari, A.1    Ceci, P.2    Ferrari, D.3    Rossi, G.L.4    Chiancone, C.5
  • 250
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells
    • Zhao G, Ceci P, Ilari A, Giangiacomo L, Laue TM, Chiancone E, Chasteen ND. 2002. Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. J Biol Chem 277:27689-27696.
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 251
    • 3042662444 scopus 로고    scopus 로고
    • Dps protects cells against multiple stresses during stationary phase
    • Nair S, Finkel SE. 2004. Dps protects cells against multiple stresses during stationary phase. J Bacteriol 186:4192-4198.
    • (2004) J Bacteriol , vol.186 , pp. 4192-4198
    • Nair, S.1    Finkel, S.E.2
  • 252
    • 0023682629 scopus 로고
    • Histone-like proteins and bacterial chromosome structure
    • Pettijohn D. 1988. Histone-like proteins and bacterial chromosome structure. J Biol Chem 263:12793-12796.
    • (1988) J Biol Chem , vol.263 , pp. 12793-12796
    • Pettijohn, D.1
  • 253
    • 0035695190 scopus 로고    scopus 로고
    • Growth-dependent DNA breakage and cell death in a gyrase mutant of Salmonella
    • Gari E, Bossi L, Gigueroa-Bossi N. 2001. Growth-dependent DNA breakage and cell death in a gyrase mutant of Salmonella. Genetics 159:1405-1414.
    • (2001) Genetics , vol.159 , pp. 1405-1414
    • Gari, E.1    Bossi, L.2    Gigueroa-Bossi, N.3
  • 254
    • 0037048702 scopus 로고    scopus 로고
    • HU: promoting or counteracting DNA compaction?
    • Dame RT, Goosen H. 2002. HU: promoting or counteracting DNA compaction? FEBS Lett 529:151-156.
    • (2002) FEBS Lett , vol.529 , pp. 151-156
    • Dame, R.T.1    Goosen, H.2
  • 257
    • 0027943344 scopus 로고
    • Macromolecular crowding effects on the interaction of DNA with Escherichia coli DNA-binding proteins: a model for bacterial nucleoid stabilization
    • Murphy LD, Zimmerman SB. 1994. Macromolecular crowding effects on the interaction of DNA with Escherichia coli DNA-binding proteins: a model for bacterial nucleoid stabilization. Biochim Biophys Acta 1219:277-284.
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 277-284
    • Murphy, L.D.1    Zimmerman, S.B.2
  • 258
    • 33750000118 scopus 로고    scopus 로고
    • Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome
    • Grainger DC, Hurd D, Goldberg MD, Busby SJW. 2006. Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome. Nucleic Acids Res 34:4642-4652.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4642-4652
    • Grainger, D.C.1    Hurd, D.2    Goldberg, M.D.3    Busby, S.J.W.4
  • 259
    • 0033053014 scopus 로고    scopus 로고
    • Identification of two new nucleoid proteins in spermidine nucleoids isolated from Escherichia coli
    • Murphy LD, Rosner JL, Zimmerman SB, Esposito D. 1999. Identification of two new nucleoid proteins in spermidine nucleoids isolated from Escherichia coli. J Bacteriol 181:3842-3844.
    • (1999) J Bacteriol , vol.181 , pp. 3842-3844
    • Murphy, L.D.1    Rosner, J.L.2    Zimmerman, S.B.3    Esposito, D.4
  • 260
    • 0030000241 scopus 로고    scopus 로고
    • Recombination-dependent growth in exonuclease-depleted recABC sbcBC strains of Escherichia coli K-12
    • Ryder L, Sharples GJ, Lloyd RG. 1996. Recombination-dependent growth in exonuclease-depleted recABC sbcBC strains of Escherichia coli K-12. Genetics 143:1101-1114.
    • (1996) Genetics , vol.143 , pp. 1101-1114
    • Ryder, L.1    Sharples, G.J.2    Lloyd, R.G.3
  • 261
    • 0035869023 scopus 로고    scopus 로고
    • Mechanism of origin unwinding: sequential binding of DnaA to double-and single-stranded DNA
    • Speck C, Messer W. 2001. Mechanism of origin unwinding: sequential binding of DnaA to double-and single-stranded DNA. EMBO J 20:1469-1476.
    • (2001) EMBO J , vol.20 , pp. 1469-1476
    • Speck, C.1    Messer, W.2
  • 262
    • 0026490232 scopus 로고
    • Opposed actions of regulatory proteins, DnaA and IciA, in opening the replication origin of Escherichia coli
    • Hwang DS, Kornberg A. 1992. Opposed actions of regulatory proteins, DnaA and IciA, in opening the replication origin of Escherichia coli. J Biol Chem 267:23087-23091.
    • (1992) J Biol Chem , vol.267 , pp. 23087-23091
    • Hwang, D.S.1    Kornberg, A.2
  • 263
    • 0027419803 scopus 로고
    • A novel binding protein of the origin of the Escherichia coli chromosome
    • Skarstad K, Thony B, Hwang DS, Kornberg A. 1993. A novel binding protein of the origin of the Escherichia coli chromosome. J Biol Chem 268:5365-5370.
    • (1993) J Biol Chem , vol.268 , pp. 5365-5370
    • Skarstad, K.1    Thony, B.2    Hwang, D.S.3    Kornberg, A.4
  • 264
    • 0036035581 scopus 로고    scopus 로고
    • IHF and HU stimulate assembly of pre-replication complexes at Escherichia coli oriC by two different mechanisms
    • Ryan VT, Grimwade JE, Nievera CJ, Leonard AC. 2002. IHF and HU stimulate assembly of pre-replication complexes at Escherichia coli oriC by two different mechanisms. Mol Microbiol 46:113-124.
    • (2002) Mol Microbiol , vol.46 , pp. 113-124
    • Ryan, V.T.1    Grimwade, J.E.2    Nievera, C.J.3    Leonard, A.C.4
  • 265
    • 0029791749 scopus 로고    scopus 로고
    • The Escherichia coli Fis protein prevents initiation of DNA replication from oriC in vitro
    • Wold S, Crooke E, Skarstad K. 1996. The Escherichia coli Fis protein prevents initiation of DNA replication from oriC in vitro. Nucleic Acids Res 24:3527-3532.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3527-3532
    • Wold, S.1    Crooke, E.2    Skarstad, K.3
  • 266
    • 0028219947 scopus 로고
    • SeqA: a negative modulator of replication initiation in E. coli
    • Lu M, Campbell JL, Boye E, Kleckner N. 1994. SeqA: a negative modulator of replication initiation in E. coli. Cell 77:413-426.
    • (1994) Cell , vol.77 , pp. 413-426
    • Lu, M.1    Campbell, J.L.2    Boye, E.3    Kleckner, N.4
  • 267
    • 8544240894 scopus 로고    scopus 로고
    • DiaA, a novel DnaAbinding protein, ensures the timely initiation of Escherichia coli chromosome replication
    • Ishida T, Akimitsu N, Kashioka T, Hatano M, Kubota T, Ogata Y, Sekimizu K, Katayama T. 2004. DiaA, a novel DnaAbinding protein, ensures the timely initiation of Escherichia coli chromosome replication. J Biol Chem 279:45546-45555.
    • (2004) J Biol Chem , vol.279 , pp. 45546-45555
    • Ishida, T.1    Akimitsu, N.2    Kashioka, T.3    Hatano, M.4    Kubota, T.5    Ogata, Y.6    Sekimizu, K.7    Katayama, T.8
  • 268
    • 0026528758 scopus 로고
    • Active partitioning of bacterial plasmids
    • Williams DB, Thomas CM. 1992. Active partitioning of bacterial plasmids. J Gen Microbiol 138:1-16.
    • (1992) J Gen Microbiol , vol.138 , pp. 1-16
    • Williams, D.B.1    Thomas, C.M.2
  • 269
    • 0024039685 scopus 로고
    • The replicative origin of the E. coli chromosome binds to cell membranes only when hemimethylated
    • Ogden GB, Pratt MJ, Schaechter M. 1988. The replicative origin of the E. coli chromosome binds to cell membranes only when hemimethylated. Cell 54:127-135.
    • (1988) Cell , vol.54 , pp. 127-135
    • Ogden, G.B.1    Pratt, M.J.2    Schaechter, M.3
  • 270
    • 84959086731 scopus 로고    scopus 로고
    • High-affinity binding of hemimethylated oriC by Escherichia coli SeqA and a newly identified factor, SeqB
    • Shakibai N, Ishidate K, Reshetnyak E, Gunji S, Kohiyama M, Rothfield L. 1998. High-affinity binding of hemimethylated oriC by Escherichia coli SeqA and a newly identified factor, SeqB. Proc Natl Acad Sci USA 95:1117-11121.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1117-11121
    • Shakibai, N.1    Ishidate, K.2    Reshetnyak, E.3    Gunji, S.4    Kohiyama, M.5    Rothfield, L.6
  • 271
    • 33745603713 scopus 로고    scopus 로고
    • The two Escherichia coli arms locate to separate cell halves
    • Wang, Liu X., X, Possoz C, Sherratt DJ. 2006. The two Escherichia coli arms locate to separate cell halves. Genes Dev 20:1727-1731.
    • (2006) Genes Dev , vol.20 , pp. 1727-1731
    • Wang, X.1    Liu, X.2    Possoz, C.3    Sherratt, D.J.4
  • 272
    • 0033546210 scopus 로고    scopus 로고
    • The organization of replication and transcription
    • Cook PR. 1999. The organization of replication and transcription. Science 184:1790-1895.
    • (1999) Science , vol.184 , pp. 1790-1895
    • Cook, P.R.1
  • 274
    • 0024594367 scopus 로고
    • Tus, the trans-acting gene required for termination of DNA replication in Escherichia coli, encodes a DNA-binding protein
    • Hill TM, Tecklenburg ML, Pelletier AJ, Kuempel PL. 1989. Tus, the trans-acting gene required for termination of DNA replication in Escherichia coli, encodes a DNA-binding protein. Proc Natl Acad Sci USA 86:1593-1597.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1593-1597
    • Hill, T.M.1    Tecklenburg, M.L.2    Pelletier, A.J.3    Kuempel, P.L.4
  • 275
    • 0024456621 scopus 로고
    • Evidence of a ter specific binding protein essential for the termination reaction of DNA replication in Escherichia coli
    • Kobayashi T, Hidaka M, Horiuchi T. 1989. Evidence of a ter specific binding protein essential for the termination reaction of DNA replication in Escherichia coli. EMBO J 8:2435-2441.
    • (1989) EMBO J , vol.8 , pp. 2435-2441
    • Kobayashi, T.1    Hidaka, M.2    Horiuchi, T.3
  • 277
    • 0033083161 scopus 로고    scopus 로고
    • Upheaval in the bacterial nucleoid: an active chromosome segregation mechanism
    • Sharpe ME. 1999. Upheaval in the bacterial nucleoid: an active chromosome segregation mechanism. Trends Genet 15:70-73.
    • (1999) Trends Genet , vol.15 , pp. 70-73
    • Sharpe, M.E.1
  • 278
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang JC. 1996. DNA topoisomerases. Annu Rev Biochem 65:835-892.
    • (1996) Annu Rev Biochem , vol.65 , pp. 835-892
    • Wang, J.C.1
  • 279
    • 0035868644 scopus 로고    scopus 로고
    • Topoisomerase IV, alone, unknots DNA in E. coli
    • Deibler RW, Rahmati S, Zechiedrich EL. 2001. Topoisomerase IV, alone, unknots DNA in E. coli. Genes Dev 15:748-761.
    • (2001) Genes Dev , vol.15 , pp. 748-761
    • Deibler, R.W.1    Rahmati, S.2    Zechiedrich, E.L.3
  • 280
    • 0037416969 scopus 로고    scopus 로고
    • Alteration of Escherichia coli topoisomerase IV to novobiocin resistance
    • Hardy CD, Cozzarelli NR. 2003. Alteration of Escherichia coli topoisomerase IV to novobiocin resistance. Antimicrob Agents Chemother 47:941-947.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 941-947
    • Hardy, C.D.1    Cozzarelli, N.R.2
  • 282
    • 0030771373 scopus 로고    scopus 로고
    • Topoisomerase IV, not gyrase, decatenates products of site-specific recombination in Escherichia coli
    • Zechiedrich EL, Khodursky AB, Cozzarelli NR. 1997. Topoisomerase IV, not gyrase, decatenates products of site-specific recombination in Escherichia coli. Genes Dev 11:2580-2592.
    • (1997) Genes Dev , vol.11 , pp. 2580-2592
    • Zechiedrich, E.L.1    Khodursky, A.B.2    Cozzarelli, N.R.3
  • 283
    • 0001731921 scopus 로고
    • Roles of supercoiled DNA structure in DNA transactions
    • Kanaar R, Cozzarelli NR. 1992. Roles of supercoiled DNA structure in DNA transactions. Curr Opin Struct Biol 2:369-379.
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 369-379
    • Kanaar, R.1    Cozzarelli, N.R.2
  • 284
    • 33750504444 scopus 로고    scopus 로고
    • Structural and physical aspects of bacterial chromosome segregation
    • Woldringh CL, Nanninga N. 2006. Structural and physical aspects of bacterial chromosome segregation. J Struct Biol 156:273-283.
    • (2006) J Struct Biol , vol.156 , pp. 273-283
    • Woldringh, C.L.1    Nanninga, N.2
  • 286
    • 21744438593 scopus 로고    scopus 로고
    • Bacterial DNA segregation by the actinlike MreB protein
    • Kruse I, Gerdes K. 2005. Bacterial DNA segregation by the actinlike MreB protein. Trends Cell Biol 15:345.
    • (2005) Trends Cell Biol , vol.15 , pp. 345
    • Kruse, I.1    Gerdes, K.2
  • 287
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse I, Moller-Jensen J, Lobner-Olesen A, Gerdes K. 2003. Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J 22:5283-5292.
    • (2003) EMBO J , vol.22 , pp. 5283-5292
    • Kruse, I.1    Moller-Jensen, J.2    Lobner-Olesen, A.3    Gerdes, K.4
  • 289
    • 0036900016 scopus 로고    scopus 로고
    • Assembly of cell division proteins at the E. coli cell center
    • Buddelmeijer N, Beckwith J. 2002. Assembly of cell division proteins at the E. coli cell center. Curr Opin Microbiol 5:553-557.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 553-557
    • Buddelmeijer, N.1    Beckwith, J.2
  • 290
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability
    • Romberg L, Levin PA. 2003. Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability. Annu Rev Microbiol 57:125-154.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 291
    • 0025848322 scopus 로고
    • Autoradiographic analysis of diaminopimelic acid incorporation in filamentous cells of Escherichia coli: repression of peptidoglycan synthesis around the nucleoid
    • Mulder E, Woldringh CL. 1991. Autoradiographic analysis of diaminopimelic acid incorporation in filamentous cells of Escherichia coli: repression of peptidoglycan synthesis around the nucleoid. J Bacteriol 173:4751-4756.
    • (1991) J Bacteriol , vol.173 , pp. 4751-4756
    • Mulder, E.1    Woldringh, C.L.2
  • 292
    • 0024720146 scopus 로고
    • Actively replicating nucleoids influence positioning of division sites in Escherichia coli filaments forming cells lacking DNA
    • Mulder E, Woldringh CL. 1989. Actively replicating nucleoids influence positioning of division sites in Escherichia coli filaments forming cells lacking DNA. J Bacteriol 171:4303-4314.
    • (1989) J Bacteriol , vol.171 , pp. 4303-4314
    • Mulder, E.1    Woldringh, C.L.2
  • 293
    • 0025813235 scopus 로고
    • Toporegulation of bacterial divisiron according to the nucleoid occlusion model
    • Woldringh CL, Mulder E, Huls PG, Vischer N. 1991. Toporegulation of bacterial divisiron according to the nucleoid occlusion model. Res Microbiol 142:309-320.
    • (1991) Res Microbiol , vol.142 , pp. 309-320
    • Woldringh, C.L.1    Mulder, E.2    Huls, P.G.3    Vischer, N.4
  • 294
    • 0035145619 scopus 로고    scopus 로고
    • Influence of the nucleoid placement of FstZ and MinE rings in Escherichia coli
    • Sun Q, Margolin W. 2001. Influence of the nucleoid placement of FstZ and MinE rings in Escherichia coli. J Bacteriol 183:1413-1422.
    • (2001) J Bacteriol , vol.183 , pp. 1413-1422
    • Sun, Q.1    Margolin, W.2
  • 295
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin DM, de Boer PA. 1999. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc Natl Acad Sci USA 96:4971-4976.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 296
    • 1542358154 scopus 로고    scopus 로고
    • A hypothesis to explain division site selection in Escherichia coli by combining nucleoid occlusion and Min
    • Norris V, Woldringh C, Mileykovskaya E. 2004. A hypothesis to explain division site selection in Escherichia coli by combining nucleoid occlusion and Min. FEBS Lett 561:3-10.
    • (2004) FEBS Lett , vol.561 , pp. 3-10
    • Norris, V.1    Woldringh, C.2    Mileykovskaya, E.3
  • 297
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
    • De Boer PA, Crossley RE, Rothfield LI. 1989. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 56:641-649.
    • (1989) Cell , vol.56 , pp. 641-649
    • De Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 298
    • 0035794706 scopus 로고    scopus 로고
    • Dynamic localization cycle of the cell division regulator MinE in Escherichia coli
    • Hale CA, Meinhardt H, de Boer PA. 2001. Dynamic localization cycle of the cell division regulator MinE in Escherichia coli. EMBO J 20:1563-1572.
    • (2001) EMBO J , vol.20 , pp. 1563-1572
    • Hale, C.A.1    Meinhardt, H.2    de Boer, P.A.3
  • 300
    • 0027467896 scopus 로고
    • Anchoring of DNA to the bacterial cytoplasmic membrane through cotranscriptional synthesis of polypeptides encoding membrane proteins for export: a mechanism of plasmid hypernegative supercoiling in mutants deficient in DNA topoisomerase I
    • Lynch A, Wang J. 1993. Anchoring of DNA to the bacterial cytoplasmic membrane through cotranscriptional synthesis of polypeptides encoding membrane proteins for export: a mechanism of plasmid hypernegative supercoiling in mutants deficient in DNA topoisomerase I. J Bacteriol 175:1645-1655.
    • (1993) J Bacteriol , vol.175 , pp. 1645-1655
    • Lynch, A.1    Wang, J.2
  • 301
    • 0026442269 scopus 로고
    • Dynamics of DNA supercoiling by transcription in E. coli
    • Cook D, Ma D, Pon M, Hearst J. 1992. Dynamics of DNA supercoiling by transcription in E. coli. Proc Natl Acad Sci USA 89: 10603-10607.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10603-10607
    • Cook, D.1    Ma, D.2    Pon, M.3    Hearst, J.4
  • 302
    • 2642672756 scopus 로고
    • Topoisomerase I mutants: the gene on pBR322 that encodes resistance to tetracycline affects plasmid DNA supercoiling
    • Pruss GJ, Drlica K. 1986. Topoisomerase I mutants: the gene on pBR322 that encodes resistance to tetracycline affects plasmid DNA supercoiling. Proc Natl Acad Sci USA 83:8952-8956.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8952-8956
    • Pruss, G.J.1    Drlica, K.2
  • 303
    • 0033587717 scopus 로고    scopus 로고
    • Gene silencing via protein-mediated subcellular localization of DNA
    • Kim S-K, Wang JC. 1999. Gene silencing via protein-mediated subcellular localization of DNA. Proc Natl Acad Sci USA 96:8557-8561.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8557-8561
    • Kim, S.-K.1    Wang, J.C.2
  • 304
    • 0030633568 scopus 로고    scopus 로고
    • RecA protein: structure, function, and role in recombinational DNA repair
    • Roca AI, Cox MM. 1997. RecA protein: structure, function, and role in recombinational DNA repair. Proc Nucleic Acid Res Mol Biol 56:129-223.
    • (1997) Proc Nucleic Acid Res Mol Biol , vol.56 , pp. 129-223
    • Roca, A.I.1    Cox, M.M.2
  • 305
    • 0028292327 scopus 로고
    • Homologous recombination: the pieces begin to fall into place
    • Clark AJ, Sandler SJ. 1994. Homologous recombination: the pieces begin to fall into place. Crit Rev Microbiol 20:125-142.
    • (1994) Crit Rev Microbiol , vol.20 , pp. 125-142
    • Clark, A.J.1    Sandler, S.J.2
  • 307
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • West SV. 1997. Processing of recombination intermediates by the RuvABC proteins. Annu Rev Genet 31:213-244.
    • (1997) Annu Rev Genet , vol.31 , pp. 213-244
    • West, S.V.1
  • 308
    • 0036683338 scopus 로고    scopus 로고
    • Genome stability and the processing of damaged replication forks by RecG
    • McGlynn P, Lloyd RG. 2002. Genome stability and the processing of damaged replication forks by RecG. Trends Genet 18:413-419
    • (2002) Trends Genet , vol.18 , pp. 413-419
    • McGlynn, P.1    Lloyd, R.G.2
  • 309
    • 0035902521 scopus 로고    scopus 로고
    • Participation of recombination proteins in rescue of arrested replication forms in UV-irradiated Escherichia coli need not involve recombination
    • Courcelle J, Hanawalt PC. 2001. Participation of recombination proteins in rescue of arrested replication forms in UV-irradiated Escherichia coli need not involve recombination. Pro Natl Acad Sci USA 98:8196-8202.
    • (2001) Pro Natl Acad Sci USA , vol.98 , pp. 8196-8202
    • Courcelle, J.1    Hanawalt, P.C.2
  • 310
    • 0035075383 scopus 로고    scopus 로고
    • How sigma docks to RNA polymerase and what sigma does
    • Burgess RR, Anthony L. 2001. How sigma docks to RNA polymerase and what sigma does. Curr Opin Microbiol 4:126-131.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 126-131
    • Burgess, R.R.1    Anthony, L.2
  • 311
    • 0037261948 scopus 로고    scopus 로고
    • The s70 family of sigma factors
    • Paget MS, Helmann JD. 2003. The s70 family of sigma factors. Genome Biol 4(1):203.
    • (2003) Genome Biol , vol.4 , Issue.1 , pp. 203
    • Paget, M.S.1    Helmann, J.D.2
  • 312
    • 0030728648 scopus 로고    scopus 로고
    • Adaptation of gene expression in stationary phase bacteria
    • Ishihama A. 1997. Adaptation of gene expression in stationary phase bacteria. Curr Opin Microbiol 7:582-588.
    • (1997) Curr Opin Microbiol , vol.7 , pp. 582-588
    • Ishihama, A.1
  • 313
    • 0242386460 scopus 로고    scopus 로고
    • Identifying global regulators in transcriptional regulatory networks in bacteria
    • Martinez A, Collado-Vides J. 2003. Identifying global regulators in transcriptional regulatory networks in bacteria. Curr Opin Microbiol 6:482-489.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 482-489
    • Martinez, A.1    Collado-Vides, J.2
  • 314
    • 34347374095 scopus 로고    scopus 로고
    • Genomic SELEX search for target promoters under the control of the PhoQP-RstBA signal relay cascade
    • Ogasawara H, Hasegawa A, Kanda E, Miki T, Yamamoto K, Ishihama A. 2007. Genomic SELEX search for target promoters under the control of the PhoQP-RstBA signal relay cascade. J Bacteriol 289:4791-4799.
    • (2007) J Bacteriol , vol.289 , pp. 4791-4799
    • Ogasawara, H.1    Hasegawa, A.2    Kanda, E.3    Miki, T.4    Yamamoto, K.5    Ishihama, A.6
  • 315
    • 34547633841 scopus 로고    scopus 로고
    • PdhR (pyruvate dehydrogenase complex regulator) controls the respiratory electron transport system in Escherichia coli
    • Ogasawara H, Ishida Y, Yamada K, Yamamoto K, Ishihama A. 2007. PdhR (pyruvate dehydrogenase complex regulator) controls the respiratory electron transport system in Escherichia coli. J Bacteriol 189:5534-5541.
    • (2007) J Bacteriol , vol.189 , pp. 5534-5541
    • Ogasawara, H.1    Ishida, Y.2    Yamada, K.3    Yamamoto, K.4    Ishihama, A.5
  • 316
    • 24344490227 scopus 로고    scopus 로고
    • Systematic search for the Cra-binding promoters using genomic SELEX system
    • Shimada T, Fujita N, Maeda M, Ishihama A. 2005. Systematic search for the Cra-binding promoters using genomic SELEX system. Genes Cells 10:907-918.
    • (2005) Genes Cells , vol.10 , pp. 907-918
    • Shimada, T.1    Fujita, N.2    Maeda, M.3    Ishihama, A.4
  • 317
    • 50149089599 scopus 로고    scopus 로고
    • Construction of 'promoter chip' for microarray analysis of regulation targets by transcription factors
    • Fukuda et al T. (ed), MHS, Nagoya, Japan
    • Yamamoto K, Ishihama A. 2007. Construction of 'promoter chip' for microarray analysis of regulation targets by transcription factors, p 135-138. In Fukuda et al T. (ed), Micro-Nano Mechatronics and Human Science. MHS, Nagoya, Japan.
    • (2007) Micro-Nano Mechatronics and Human Science , pp. 135-138
    • Yamamoto, K.1    Ishihama, A.2
  • 319
    • 24344447800 scopus 로고    scopus 로고
    • Immobilization of Escherichia coli RNA polymerase and localization of binding sites by use of chromatin immunoprecipitation and microarrays
    • Herring CD, Raffaelle M, Allen TE, Kanin EI, Landick R, Ansari AZ, Palsson BO. 2005. Immobilization of Escherichia coli RNA polymerase and localization of binding sites by use of chromatin immunoprecipitation and microarrays. J Bacteriol 187:6166-6174.
    • (2005) J Bacteriol , vol.187 , pp. 6166-6174
    • Herring, C.D.1    Raffaelle, M.2    Allen, T.E.3    Kanin, E.I.4    Landick, R.5    Ansari, A.Z.6    Palsson, B.O.7
  • 320
    • 0021700772 scopus 로고
    • Bacterial regulation: global regulatory networks
    • Gottesman S. 1984. Bacterial regulation: global regulatory networks. Annu Rev Genet 18:415-441.
    • (1984) Annu Rev Genet , vol.18 , pp. 415-441
    • Gottesman, S.1
  • 321
    • 0027236999 scopus 로고
    • Transcriptional regulation by cAMP and its receptor protein
    • Kolb A, Busby S, Buc H, Garges S, Adhya S. 1993. Transcriptional regulation by cAMP and its receptor protein. Annu Rev Biochem 62:749-795.
    • (1993) Annu Rev Biochem , vol.62 , pp. 749-795
    • Kolb, A.1    Busby, S.2    Buc, H.3    Garges, S.4    Adhya, S.5
  • 322
    • 0017145525 scopus 로고
    • Cyclic adenosime 5'-monophosphate in Escherichia coli
    • Pastan I, Adhya S. 1976. Cyclic adenosime 5'-monophosphate in Escherichia coli. Bacteriol Rev 40:527-551.
    • (1976) Bacteriol Rev , vol.40 , pp. 527-551
    • Pastan, I.1    Adhya, S.2
  • 323
    • 40649089205 scopus 로고    scopus 로고
    • Dissecting the logical types of network control in gene expression profiles
    • Marr C, Geertz M, M-Hutt T, Muskelishvili G. 2008. Dissecting the logical types of network control in gene expression profiles. BMC Syst Biol 2:18.
    • (2008) BMC Syst Biol , vol.2 , pp. 18
    • Marr, C.1    Geertz, M.2    M.-Hutt, T.3    Muskelishvili, G.4
  • 324
    • 0030896970 scopus 로고    scopus 로고
    • RNA polymerase β' subunit: a target of DNA binding-independent activation
    • Miller A, Wood D, Ebright RH, Rothman-Denes LB. 1997. RNA polymerase β' subunit: a target of DNA binding-independent activation. Science 275:1655-1657.
    • (1997) Science , vol.275 , pp. 1655-1657
    • Miller, A.1    Wood, D.2    Ebright, R.H.3    Rothman-Denes, L.B.4
  • 325
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all twocomponent signal transduction systems from Escherichia coli
    • Yamamoto K, Hirao K, Oshima T, Aiba H, Utsumi R, Ishihama A. 2005. Functional characterization in vitro of all twocomponent signal transduction systems from Escherichia coli. J Biol Chem 280:1448-1456.
    • (2005) J Biol Chem , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5    Ishihama, A.6
  • 326
    • 84959148332 scopus 로고    scopus 로고
    • The distribution of RNA polymerase in Escherichia coli is dynamic and sensitive to environmental cues
    • Cabrera JE, Jin DJ. 2003. The distribution of RNA polymerase in Escherichia coli is dynamic and sensitive to environmental cues. Mol Microbiol 6:165-170.
    • (2003) Mol Microbiol , vol.6 , pp. 165-170
    • Cabrera, J.E.1    Jin, D.J.2
  • 327
    • 0034651795 scopus 로고    scopus 로고
    • Compartmentalization of transcription and translation in Bacillus subtilis
    • Lewis P, Thanker SD, Errington J. 2000. Compartmentalization of transcription and translation in Bacillus subtilis. EMBO J 19:710-718.
    • (2000) EMBO J , vol.19 , pp. 710-718
    • Lewis, P.1    Thanker, S.D.2    Errington, J.3
  • 328
    • 0017760149 scopus 로고
    • Biosynthesis of RNA polymerase in Escherichia coli: intracellular distribution of RNA polymerase subunits between nucleoid and cytoplasm
    • Saitoh T, Ishihama A. 1977. Biosynthesis of RNA polymerase in Escherichia coli: intracellular distribution of RNA polymerase subunits between nucleoid and cytoplasm. J Mol Biol 115:403-416.
    • (1977) J Mol Biol , vol.115 , pp. 403-416
    • Saitoh, T.1    Ishihama, A.2
  • 329
    • 0001481089 scopus 로고
    • Bacterial chromosome structure
    • Eckstein F and Lilley DMJ (ed), Springer, Berlin, Germany
    • Pettijohn D. 1990. Bacterial chromosome structure, p 152-162. In Eckstein F and Lilley DMJ (ed), Nucleic Acids and Molecular Biology. Springer, Berlin, Germany.
    • (1990) Nucleic Acids and Molecular Biology , pp. 152-162
    • Pettijohn, D.1
  • 330
    • 0016771381 scopus 로고
    • Localization of transcribing genes in the bacterial cell by means of high resolution autoradiography
    • Ryter A, Chang A. 1955. Localization of transcribing genes in the bacterial cell by means of high resolution autoradiography. J Mol Biol 98:797-810.
    • (1955) J Mol Biol , vol.98 , pp. 797-810
    • Ryter, A.1    Chang, A.2
  • 331
    • 0023117639 scopus 로고
    • Use of site specific recombination as a probe of DNA structure and metabolism in vivo
    • Bliska J, Cozzarelli N. 1987. Use of site specific recombination as a probe of DNA structure and metabolism in vivo. J Mol Biol 194:205-218.
    • (1987) J Mol Biol , vol.194 , pp. 205-218
    • Bliska, J.1    Cozzarelli, N.2
  • 332
    • 0043260772 scopus 로고
    • Roles of DNA topoisomerases in bacterial chromosome structure and function
    • Drlica K and Riley M (ed), American Society for Microbiology, Washington, DC
    • Drlica K, Pruss G, Burger R Franco R, Hsieh L-S, Berger B. 1990. Roles of DNA topoisomerases in bacterial chromosome structure and function, p 195-204. In Drlica K and Riley M (ed), The Bacterial Chromosome. American Society for Microbiology, Washington, DC.
    • (1990) The Bacterial Chromosome , pp. 195-204
    • Drlica, K.1    Pruss, G.2    Burger, R.3    Franco, R.4    Hsieh, L.-S.5    Berger, B.6
  • 333
    • 0035875344 scopus 로고    scopus 로고
    • Massive parallel analysis of the binding specificity of histone-like protein HU to single-and double-stranded DNA with generic oligodeoxyribonucleotide microchips
    • Krylov AS, Zasedateleva OA, Prokopenko DV, Rouviere-Yaniv J, Mirzabekov AD. 2001. Massive parallel analysis of the binding specificity of histone-like protein HU to single-and double-stranded DNA with generic oligodeoxyribonucleotide microchips. Nucleic Acids Res 29:2654-2660.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2654-2660
    • Krylov, A.S.1    Zasedateleva, O.A.2    Prokopenko, D.V.3    Rouviere-Yaniv, J.4    Mirzabekov, A.D.5
  • 334
    • 0035075425 scopus 로고    scopus 로고
    • Control of transcription by nucleoid proteins
    • McLeod SM, Johnson RC. 2001. Control of transcription by nucleoid proteins. Curr Opin Microbiol 4:348-349.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 348-349
    • McLeod, S.M.1    Johnson, R.C.2


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