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Volumn 56, Issue 4, 2005, Pages 858-870

The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FACTOR FOR INVERSION STIMULATION; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; HU PROTEIN; NUCLEOID ASSOCIATED PROTEIN; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 18444369954     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04598.x     Document Type: Short Survey
Times cited : (314)

References (110)
  • 1
    • 0031970775 scopus 로고    scopus 로고
    • Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo
    • Afflerbach, H., Schroder, O., and Wagner, R. (1998) Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo. Mol Microbiol 28: 641-653.
    • (1998) Mol Microbiol , vol.28 , pp. 641-653
    • Afflerbach, H.1    Schroder, O.2    Wagner, R.3
  • 3
    • 0037832291 scopus 로고    scopus 로고
    • Stretching DNA and RNA to probe their interactions with proteins
    • Allemand, J.F., Bensimon, D., and Croquette, V. (2003) Stretching DNA and RNA to probe their interactions with proteins. Curr Opin Struct Biol 13: 266-274.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 266-274
    • Allemand, J.F.1    Bensimon, D.2    Croquette, V.3
  • 4
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron, M., Link, A.J., Furlong, D., and Kolter, R. (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6: 2646-2654.
    • (1992) Genes Dev , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 5
    • 0037381991 scopus 로고    scopus 로고
    • Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor
    • Amit, R., Oppenheim, A.B., and 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
  • 6
    • 4143104537 scopus 로고    scopus 로고
    • Single molecule elasticity measurements: A biophysical approach to bacterial nucleoid organization
    • Amit, R., Oppenheim, A.B., and Stavans, J. (2004) Single molecule elasticity measurements: a biophysical approach to bacterial nucleoid organization. Biophys J 87: 1392-1393.
    • (2004) Biophys J , vol.87 , pp. 1392-1393
    • Amit, R.1    Oppenheim, A.B.2    Stavans, J.3
  • 7
    • 0034703060 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12. The effects of integration host factor
    • Arfin, S.M., Long, A.D., Ito, E.T., Tolleri, L., Riehle, M.M., Paegle, E.S., and Hatfield, G.W. (2000) Global gene expression profiling in Escherichia coli K12. The effects of integration host factor. J Biol Chem 275: 29672-29684.
    • (2000) J Biol Chem , vol.275 , pp. 29672-29684
    • Arfin, S.M.1    Long, A.D.2    Ito, E.T.3    Tolleri, L.4    Riehle, M.M.5    Paegle, E.S.6    Hatfield, G.W.7
  • 8
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam, T.A., Iwata, A., Nishimura, A., Ueda, S., and 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.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 9
    • 0037008678 scopus 로고    scopus 로고
    • The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids
    • Balandina, A., Kamashev, D., and Rouviere-Yaniv, J. (2002) The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids. J Biol Chem 277: 27622-27628.
    • (2002) J Biol Chem , vol.277 , pp. 27622-27628
    • Balandina, A.1    Kamashev, D.2    Rouviere-Yaniv, J.3
  • 10
    • 0038136948 scopus 로고    scopus 로고
    • Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein
    • Beloin, C., Jeusset, J., Revet, B., Mirambeau, G., Le Hegarat, F., and Le Cam, E. (2003) Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein. J Biol Chem 278: 5333-5342.
    • (2003) J Biol Chem , vol.278 , pp. 5333-5342
    • Beloin, C.1    Jeusset, J.2    Revet, B.3    Mirambeau, G.4    Le Hegarat, F.5    Le Cam, E.6
  • 11
    • 0037336248 scopus 로고    scopus 로고
    • The H-NS dimerization domain defines a new fold contributing to DNA recognition
    • Bloch, V., Yang, Y., Margeat, E., Chavanieu, A., Auge, M.T., Robert, B., et al. (2003) The H-NS dimerization domain defines a new fold contributing to DNA recognition. Nat Struct Biol 10: 212-218.
    • (2003) Nat Struct Biol , vol.10 , pp. 212-218
    • Bloch, V.1    Yang, Y.2    Margeat, E.3    Chavanieu, A.4    Auge, M.T.5    Robert, B.6
  • 12
    • 0033818258 scopus 로고    scopus 로고
    • Suppression of FNR-dependent 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, D.F., Cole, J.A., and Busby, S.J. (2000) Suppression of FNR-dependent 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.3
  • 13
    • 0023041804 scopus 로고
    • Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like structures with altered DNA helical pitch
    • Broyles, S.S., and Pettijohn, D.E. (1986) Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like 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
  • 14
    • 0029970157 scopus 로고    scopus 로고
    • Visualizing protein-nucleic acid interactions on a large scale with the scanning force microscope
    • Bustamante, C., and Rivetti, C. (1996) Visualizing protein-nucleic acid interactions on a large scale with the scanning force microscope. Annu Rev Biophys Biomol Struct 25: 395-429.
    • (1996) Annu Rev Biophys Biomol Struct , vol.25 , pp. 395-429
    • Bustamante, C.1    Rivetti, C.2
  • 15
    • 0346887121 scopus 로고    scopus 로고
    • The distribution of RNA polymerase in Escherichia coli is dynamic and sensitive to environmental cues
    • Cabrera, J.E., and Jin, D.J. (2003) The distribution of RNA polymerase in Escherichia coli is dynamic and sensitive to environmental cues. Mol Microbiol 50: 1493-1505.
    • (2003) Mol Microbiol , vol.50 , pp. 1493-1505
    • Cabrera, J.E.1    Jin, D.J.2
  • 16
    • 3042845898 scopus 로고    scopus 로고
    • The bacterial condensin MukBEF compacts DNA into a repetitive, stable structure
    • Case, R.B., Chang, Y.P., Smith, S.B., Gore, J., Cozzarelli, N.R., and Bustamante, C. (2004) The bacterial condensin MukBEF compacts DNA into a repetitive, stable structure. Science 305: 222-227.
    • (2004) Science , vol.305 , pp. 222-227
    • Case, R.B.1    Chang, Y.P.2    Smith, S.B.3    Gore, J.4    Cozzarelli, N.R.5    Bustamante, C.6
  • 17
    • 0028901705 scopus 로고
    • HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps
    • Castaing, B., Zelwer, C., Laval, J., and Boiteux, S. (1995) HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps. J Biol Chem 270: 10291-10296.
    • (1995) J Biol Chem , vol.270 , pp. 10291-10296
    • Castaing, B.1    Zelwer, C.2    Laval, J.3    Boiteux, S.4
  • 18
    • 0242289355 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae
    • Cerdan, R., Bloch, V., Yang, Y., Bertin, P., Dumas, C., Rimsky, S., et al. (2003) Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae. J Mol Biol 334: 179-185.
    • (2003) J Mol Biol , vol.334 , pp. 179-185
    • Cerdan, R.1    Bloch, V.2    Yang, Y.3    Bertin, P.4    Dumas, C.5    Rimsky, S.6
  • 19
    • 0035782861 scopus 로고    scopus 로고
    • Polymer-mediated compaction and internal dynamics of isolated Escherichia coli nucleoids
    • Cunha, S., Woldringh, C.L., and 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
  • 20
    • 0037048702 scopus 로고    scopus 로고
    • HU: Promoting or counteracting DNA compaction?
    • Dame, R.T., and Goosen, N. (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, N.2
  • 21
    • 0344550515 scopus 로고    scopus 로고
    • On the role of H-NS in the organization of bacterial chromatin: From bulk to single molecules and back
    • Dame, R.T., and Wuite, G.J. (2003) On the role of H-NS in the organization of bacterial chromatin: from bulk to single molecules and back. Biophys J 85: 4146-4148.
    • (2003) Biophys J , vol.85 , pp. 4146-4148
    • Dame, R.T.1    Wuite, G.J.2
  • 22
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame, R.T., Wyman, C., and 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
  • 23
    • 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, R.T., Wyman, C., Wurm, R., Wagner, R., and 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    Wurm, R.3    Wagner, R.4    Goosen, N.5
  • 25
    • 0016018740 scopus 로고
    • Electron microscopic studies on the folded chromosome of Escherichia coli
    • Delius, H., and Worcel, A. (1974) Electron microscopic studies on the folded chromosome of Escherichia coli. Cold Spring Harb Symp Quant Biol 38: 53-58.
    • (1974) Cold Spring Harb Symp Quant Biol , vol.38 , pp. 53-58
    • Delius, H.1    Worcel, A.2
  • 26
    • 1542618333 scopus 로고    scopus 로고
    • Transcription-induced barriers to supercoil diffusion in the Salmonella typhimurium chromosome
    • Deng, S., Stein, R.A., and Higgins, N.P. (2004) Transcription-induced barriers to supercoil diffusion in the Salmonella typhimurium chromosome. Proc Natl Acad Sci USA 101: 3398-3403.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3398-3403
    • Deng, S.1    Stein, R.A.2    Higgins, N.P.3
  • 27
    • 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., and Schnetz, K. (2004) The histone-like nucleoid structuring protein H-NS represses the Escherichia coli bgl operon downstream of the promoter. Mol Microbiol 52: 589-600.
    • (2004) Mol Microbiol , vol.52 , pp. 589-600
    • Dole, S.1    Nagarajavel, V.2    Schnetz, K.3
  • 28
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: A universal regulator for a dynamic genome
    • Dorman, C.J. (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.J.1
  • 29
    • 0033104294 scopus 로고    scopus 로고
    • Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria
    • Dorman, C.J., Hinton, J.C., and 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.2    Free, A.3
  • 30
    • 0017837314 scopus 로고
    • The compaction of DNA helices into either continuous supercoils or folded-fiber rods and toroids
    • Eickbush, T.H., and Moudrianakis, E.N. (1978) The compaction of DNA helices into either continuous supercoils or folded-fiber rods and toroids. Cell 13: 295-306.
    • (1978) Cell , vol.13 , pp. 295-306
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 31
    • 0036928821 scopus 로고    scopus 로고
    • H-NS oligomerization domain structure reveals the mechanism for high order self association of the intact protein
    • Esposito, D., Petrovic, A., Harris, R., Ono, S., Eccleston, J.F., Mbabaali, A., et al. (2002) H-NS oligomerization domain structure reveals the mechanism for high order self association of the intact protein. J Mol Biol 324: 841-850.
    • (2002) J Mol Biol , vol.324 , pp. 841-850
    • Esposito, D.1    Petrovic, A.2    Harris, R.3    Ono, S.4    Eccleston, J.F.5    Mbabaali, A.6
  • 32
    • 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., and 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
  • 33
    • 0346750971 scopus 로고    scopus 로고
    • Single-molecule studies of DNA architectural changes induced by regulatory proteins
    • Finzi, L., and Dunlap, D. (2003) Single-molecule studies of DNA architectural changes induced by regulatory proteins. Methods Enzymol 370: 369-378.
    • (2003) Methods Enzymol , vol.370 , pp. 369-378
    • Finzi, L.1    Dunlap, D.2
  • 34
    • 0035283138 scopus 로고    scopus 로고
    • Regulated phase transitions of bacterial chromatin: A non-enzymatic pathway for generic DNA protection
    • Frenkiel-Krispin, D., Levin-Zaidman, S., Shimoni, E., Wolf, S.G., Wachtel, E.J., Arad, T., et al. (2001) Regulated phase transitions of bacterial chromatin: a non-enzymatic pathway for generic DNA protection. EMBO J 20: 1184-1191.
    • (2001) EMBO J , vol.20 , pp. 1184-1191
    • Frenkiel-Krispin, D.1    Levin-Zaidman, S.2    Shimoni, E.3    Wolf, S.G.4    Wachtel, E.J.5    Arad, T.6
  • 35
    • 0043166926 scopus 로고    scopus 로고
    • Complex regulation of csgD promoter activity by global regulatory proteins
    • Gerstel, U., Park, C., and Romling, U. (2003) Complex regulation of csgD promoter activity by global regulatory proteins. Mol Microbiol 49: 639-654.
    • (2003) Mol Microbiol , vol.49 , pp. 639-654
    • Gerstel, U.1    Park, C.2    Romling, U.3
  • 36
    • 0028922082 scopus 로고
    • The regulation of transcription initiation by integration host factor
    • Goosen, N., and van de Putte, P. (1995) The regulation of transcription initiation by integration host factor. Mol Microbiol 16: 1-7.
    • (1995) Mol Microbiol , vol.16 , pp. 1-7
    • Goosen, N.1    Van De Putte, P.2
  • 37
    • 0035119398 scopus 로고    scopus 로고
    • SMC proteins in bacteria: Condensation motors for chromosome segregation?
    • Graumann, P.L. (2001) SMC proteins in bacteria: condensation motors for chromosome segregation? Biochimie 83: 53-59.
    • (2001) Biochimie , vol.83 , pp. 53-59
    • Graumann, P.L.1
  • 38
    • 0012911305 scopus 로고
    • Visualization of prokaryotic DNA in a regularly condensed chromatin-like fiber
    • Griffith, J.D. (1976) Visualization of prokaryotic DNA in a regularly condensed chromatin-like fiber. Proc Natl Acad Sci USA 73: 563-567.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 563-567
    • Griffith, J.D.1
  • 39
    • 0035366378 scopus 로고    scopus 로고
    • Single-molecule fluorescence methods for the study of nucleic acids
    • Ha, T. (2001) Single-molecule fluorescence methods for the study of nucleic acids. Curr Opin Struct Biol 11: 287-292.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 287-292
    • Ha, T.1
  • 40
    • 0026542543 scopus 로고
    • The apical localization of transcribing RNA polymerases on supercoiled DNA prevents their rotation around the template
    • ten Heggeler-Bordier, B., Wahli, W., Adrian, M., Stasiak, A., and Dubochet, J. (1992) The apical localization of transcribing RNA polymerases on supercoiled DNA prevents their rotation around the template. EMBO J 11: 667-672.
    • (1992) EMBO J , vol.11 , pp. 667-672
    • Ten Heggeler-Bordier, B.1    Wahli, W.2    Adrian, M.3    Stasiak, A.4    Dubochet, J.5
  • 42
    • 0023833060 scopus 로고
    • A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli
    • Higgins, C.F., Dorman, C.J., Stirling, D.A., Waddell, L., Booth, I.R., May, G., and Bremer, E. (1988) A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli. Cell 52: 569-584.
    • (1988) Cell , vol.52 , pp. 569-584
    • Higgins, C.F.1    Dorman, C.J.2    Stirling, D.A.3    Waddell, L.4    Booth, I.R.5    May, G.6    Bremer, E.7
  • 43
    • 0029863159 scopus 로고    scopus 로고
    • Surveying a supercoil domain by using the gamma delta resolution system in Salmonella typhimurium
    • Higgins, N.P., Yang, X., Fu, Q., and Roth, J.R. (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
  • 44
    • 0035312659 scopus 로고    scopus 로고
    • Recent advances in FRET: Distance determination in protein-DNA complexes
    • Hillisch, A., Lorenz, M., and Diekmann, S. (2001) Recent advances in FRET: distance determination in protein-DNA complexes. Curr Opin Struct Biol 11: 201-207.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 201-207
    • Hillisch, A.1    Lorenz, M.2    Diekmann, S.3
  • 45
    • 0035816212 scopus 로고    scopus 로고
    • Specific and non-specific interactions of integration host factor with DNA: Thermodynamic evidence for disruption of multiple IHF surface salt-bridges coupled to DNA binding
    • Holbrook, J.A., Tsodikov, O.V., Saecker, R.M., and Record, M.T., Jr (2001) Specific and non-specific interactions of integration host factor with DNA: thermodynamic evidence for disruption of multiple IHF surface salt-bridges coupled to DNA binding. J Mol Biol 310: 379-401.
    • (2001) J Mol Biol , vol.310 , pp. 379-401
    • Holbrook, J.A.1    Tsodikov, O.V.2    Saecker, R.M.3    Record Jr., M.T.4
  • 46
    • 0035047678 scopus 로고    scopus 로고
    • Large-scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid-associated protein, H-NS
    • Hommais, F., Krin, E., Laurent-Winter, C., Soutourina, O., Malpertuy, A., Le Caer, J.P., et al. (2001) Large-scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid-associated protein, H-NS. Mol Microbiol 40: 20-36.
    • (2001) Mol Microbiol , vol.40 , pp. 20-36
    • Hommais, F.1    Krin, E.2    Laurent-Winter, C.3    Soutourina, O.4    Malpertuy, A.5    Le Caer, J.P.6
  • 47
    • 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
  • 48
    • 0033591426 scopus 로고    scopus 로고
    • An Lrp-type transcriptional regulator from Agrobacterium tumefaciens condenses more than 100 nucleotides of DNA into globular nucleoprotein complexes
    • Jafri, S., Evoy, S., Cho, K., Craighead, H.G., and Winans, S.C. (1999) An Lrp-type transcriptional regulator from Agrobacterium tumefaciens condenses more than 100 nucleotides of DNA into globular nucleoprotein complexes. J Mol Biol 288: 811-824.
    • (1999) J Mol Biol , vol.288 , pp. 811-824
    • Jafri, S.1    Evoy, S.2    Cho, K.3    Craighead, H.G.4    Winans, S.C.5
  • 49
    • 0034416406 scopus 로고    scopus 로고
    • The histone-like protein HU binds specifically to DNA recombination and repair intermediates
    • Kamashev, D., and Rouviere-Yaniv, J. (2000) The histone-like protein HU binds specifically to DNA recombination and repair intermediates. EMBO J 19: 6527-6535.
    • (2000) EMBO J , vol.19 , pp. 6527-6535
    • Kamashev, D.1    Rouviere-Yaniv, J.2
  • 50
    • 0033214062 scopus 로고    scopus 로고
    • The binding motif recognized by HU on both nicked and cruciform DNA
    • Kamashev, D., Balandina, A., and Rouviere-Yaniv, J. (1999) The binding motif recognized by HU on both nicked and cruciform DNA. EMBO J 18: 5434-5444.
    • (1999) EMBO J , vol.18 , pp. 5434-5444
    • Kamashev, D.1    Balandina, A.2    Rouviere-Yaniv, J.3
  • 51
    • 0017045430 scopus 로고
    • Electron microscopy of membrane-free folded chromosomes from Escherichia coli
    • Kavenoff, R., and Bowen, B.C. (1976) Electron microscopy of membrane-free folded chromosomes from Escherichia coli. Chromosoma 59: 89-101.
    • (1976) Chromosoma , vol.59 , pp. 89-101
    • Kavenoff, R.1    Bowen, B.C.2
  • 52
    • 0023958011 scopus 로고
    • About the organisation of condensed and decondensed non-eukaryotic DNA and the concept of vegetative DNA (a critical review)
    • Kellenberger, E. (1988) About the organisation of condensed and decondensed non-eukaryotic DNA and the concept of vegetative DNA (a critical review). Biophys Chem 29: 51-62.
    • (1988) Biophys Chem , vol.29 , pp. 51-62
    • Kellenberger, E.1
  • 53
    • 4344716137 scopus 로고    scopus 로고
    • A global role for Fis in the transcriptional control of metabolism and type III secretion in Salmonella enterica serovar Typhimurium
    • Kelly, A., Goldberg, M.D., Carroll, R.K., Danino, V., Hinton, J.C., and Dorman, C.J. (2004) A global role for Fis in the transcriptional control of metabolism and type III secretion in Salmonella enterica serovar Typhimurium. Microbiology 150: 2037-2053.
    • (2004) Microbiology , vol.150 , pp. 2037-2053
    • Kelly, A.1    Goldberg, M.D.2    Carroll, R.K.3    Danino, V.4    Hinton, J.C.5    Dorman, C.J.6
  • 54
    • 0025962021 scopus 로고
    • Three-dimensional structure of the E. coli DNA-binding protein FIS
    • Kostrewa, D., Granzin, J., Koch, C., Choe, H.W., Raghunathan, S., Wolf, W., et al. (1991) Three-dimensional structure of the E. coli DNA-binding protein FIS. Nature 349: 178-180.
    • (1991) Nature , vol.349 , pp. 178-180
    • Kostrewa, D.1    Granzin, J.2    Koch, C.3    Choe, H.W.4    Raghunathan, S.5    Wolf, W.6
  • 55
    • 0026749182 scopus 로고
    • Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution
    • Kostrewa, D., Granzin, J., Stock, D., Choe, H.W., Labahn, J., and Saenger, W. (1992) Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution. J Mol Biol 226: 209-226.
    • (1992) J Mol Biol , vol.226 , pp. 209-226
    • Kostrewa, D.1    Granzin, J.2    Stock, D.3    Choe, H.W.4    Labahn, J.5    Saenger, W.6
  • 56
    • 0024297575 scopus 로고
    • Curved helix segments can uniquely orient the topology of supertwisted DNA
    • Laundon, C.H., and Griffith, J.D. (1988) Curved helix segments can uniquely orient the topology of supertwisted DNA. Cell 52: 545-549.
    • (1988) Cell , vol.52 , pp. 545-549
    • Laundon, C.H.1    Griffith, J.D.2
  • 57
    • 0141482089 scopus 로고    scopus 로고
    • Supercoiling and denaturation in Gal repressor/heat unstable nucleoid protein (HU)-mediated DNA looping
    • Lia, G., Bensimon, D., Croquette, V., Allemand, J.F., Dunlap, D., Lewis, D.E., et al. (2003) Supercoiling and denaturation in Gal repressor/heat unstable nucleoid protein (HU)-mediated DNA looping. Proc Natl Acad Sci USA 100: 11373-11377.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11373-11377
    • Lia, G.1    Bensimon, D.2    Croquette, V.3    Allemand, J.F.4    Dunlap, D.5    Lewis, D.E.6
  • 58
    • 0016613916 scopus 로고
    • Yeast chromatin subunit structure
    • Lohr, D., and Van Holde, K.E. (1975) Yeast chromatin subunit structure. Science 188: 165-166.
    • (1975) Science , vol.188 , pp. 165-166
    • Lohr, D.1    Van Holde, K.E.2
  • 59
    • 0033485813 scopus 로고    scopus 로고
    • Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer
    • Lorenz, M., Hillisch, A., Goodman, S.D., and Diekmann, S. (1999) Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer. Nucleic Acids Res 27: 4619-4625.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4619-4625
    • Lorenz, M.1    Hillisch, A.2    Goodman, S.D.3    Diekmann, S.4
  • 60
    • 0030847091 scopus 로고    scopus 로고
    • Isolation and characterization of spermidine nucleoids from Escherichia coli
    • Murphy, L.D., and Zimmerman, S.B. (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.D.1    Zimmerman, S.B.2
  • 61
    • 2342454974 scopus 로고    scopus 로고
    • Dual architectural roles of HU: Formation of flexible hinges and rigid filaments
    • van Noort, J., Verbrugge, S., Goosen, N., Dekker, C., and Dame, R.T. (2004) Dual architectural roles of HU: formation of flexible hinges and rigid filaments. Proc Natl Acad Sci USA 101: 6969-6974.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6969-6974
    • Van Noort, J.1    Verbrugge, S.2    Goosen, N.3    Dekker, C.4    Dame, R.T.5
  • 62
    • 0029165965 scopus 로고
    • Hypothesis: Chromosome separation in Escherichia coli involves autocatalytic gene expression, transertion and membrane-domain formation
    • Norris, V. (1995) Hypothesis: chromosome separation in Escherichia coli involves autocatalytic gene expression, transertion and membrane-domain formation. Mol Microbiol 16: 1051-1057.
    • (1995) Mol Microbiol , vol.16 , pp. 1051-1057
    • Norris, V.1
  • 63
    • 0032514107 scopus 로고    scopus 로고
    • Osmotic compaction of supercoiled DNA into a bacterial nucleoid
    • Odijk, T. (1998) Osmotic compaction of supercoiled DNA into a bacterial nucleoid. Biophys Chem 73: 23-29.
    • (1998) Biophys Chem , vol.73 , pp. 23-29
    • Odijk, T.1
  • 64
    • 0015964401 scopus 로고
    • Spheroid chromatin units (v bodies)
    • Olins, A.L., and Olins, D.E. (1974) Spheroid chromatin units (v bodies). Science 183: 330-332.
    • (1974) Science , vol.183 , pp. 330-332
    • Olins, A.L.1    Olins, D.E.2
  • 65
    • 19244372639 scopus 로고    scopus 로고
    • Variable structures of Fis-DNA complexes determined by flanking DNA-protein contacts
    • Pan, C.Q., Finkel, S.E., Cramton, S.E., Feng, J.A., Sigman, D.S., and Johnson, R.C. (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.A.4    Sigman, D.S.5    Johnson, R.C.6
  • 66
    • 0020445968 scopus 로고
    • Structure and properties of the bacterial nucleoid
    • Pettijohn, D.E. (1982) Structure and properties of the bacterial nucleoid. Cell 30: 667-669.
    • (1982) Cell , vol.30 , pp. 667-669
    • Pettijohn, D.E.1
  • 67
    • 0033515646 scopus 로고    scopus 로고
    • Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA
    • Pinson, V., Takahashi, M., and Rouviere-Yaniv, J. (1999) Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA. J Mol Biol 287: 485-497.
    • (1999) J Mol Biol , vol.287 , pp. 485-497
    • Pinson, V.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 69
    • 3142774839 scopus 로고    scopus 로고
    • Topological domain structure of the Escherichia coli chromosome
    • Postow, L., Hardy, C.D., Arsuaga, J., and Cozzarelli, N.R. (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    Arsuaga, J.3    Cozzarelli, N.R.4
  • 71
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex: A protein-induced DNA U-turn
    • Rice, P.A., Yang, S., Mizuuchi, K., and Nash, H.A. (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
  • 72
    • 1842453825 scopus 로고    scopus 로고
    • Structure of the histone-like protein H-NS and its role in regulation and genome superstructure
    • Rimsky, S. (2004) Structure of the histone-like protein H-NS and its role in regulation and genome superstructure. Curr Opin Microbiol 7: 109-114.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 109-114
    • Rimsky, S.1
  • 73
    • 0035725521 scopus 로고    scopus 로고
    • A molecular mechanism for the repression of transcription by the H-NS protein
    • Rimsky, S., Zuber, F., Buckle, M., and Buc, H. (2001) A molecular mechanism for the repression of transcription by the H-NS protein. Mol Microbiol 42: 1311-1323.
    • (2001) Mol Microbiol , vol.42 , pp. 1311-1323
    • Rimsky, S.1    Zuber, F.2    Buckle, M.3    Buc, H.4
  • 74
    • 0018405881 scopus 로고
    • E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA
    • Rouviere-Yaniv, J., Yaniv, M., and Germond, J.E. (1979) E. coli DNA binding protein HU forms nucleosomelike 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
  • 75
    • 3342959174 scopus 로고    scopus 로고
    • Modulation of DNA conformations through the formation of alternative high-order HU-DNA complexes
    • Sagi, D., Friedman, N., Vorgias, C., Oppenheim, A.B., and Stavans, J. (2004) Modulation of DNA conformations through the formation of alternative high-order HU-DNA complexes. J Mol Biol 341: 419-428.
    • (2004) J Mol Biol , vol.341 , pp. 419-428
    • Sagi, D.1    Friedman, N.2    Vorgias, C.3    Oppenheim, A.B.4    Stavans, J.5
  • 77
    • 0038690473 scopus 로고    scopus 로고
    • Control of rRNA expression in Escherichia coli
    • Schneider, D.A., Ross, W., and Course, R.L. (2003) Control of rRNA expression in Escherichia coli. Curr Opin Microbiol 6: 151-156.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 151-156
    • Schneider, D.A.1    Ross, W.2    Course, R.L.3
  • 78
    • 0034685608 scopus 로고    scopus 로고
    • The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex
    • Schroder, O., and Wagner, R. (2000) The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex. J Mol Biol 298: 737-748.
    • (2000) J Mol Biol , vol.298 , pp. 737-748
    • Schroder, O.1    Wagner, R.2
  • 79
    • 0036293872 scopus 로고    scopus 로고
    • Direct atomic force microscopy visualization of integration host factor-induced DNA bending structure of the promoter regulatory region on the Pseudomonas TOL plasmid
    • Seong, G.H., Kobatake, E., Miura, K., Nakazawa, A., and Aizawa, M. (2002) Direct atomic force microscopy visualization of integration host factor-induced DNA bending structure of the promoter regulatory region on the Pseudomonas TOL plasmid. Biochem Biophys Res Commun 291: 361-366.
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 361-366
    • Seong, G.H.1    Kobatake, E.2    Miura, K.3    Nakazawa, A.4    Aizawa, M.5
  • 80
    • 0029610588 scopus 로고
    • Characterization of the binding of HU and IHF, homologous histone-like proteins of Escherichia coli, to curved and uncurved DNA
    • Shimizu, M., Miyake, M., Kanke, F., Matsumoto, U., and Shindo, H. (1995) Characterization of the binding of HU and IHF, homologous histone-like proteins of Escherichia coli, to curved and uncurved DNA. Biochim Biophys Acta 1264: 330-336.
    • (1995) Biochim Biophys Acta , vol.1264 , pp. 330-336
    • Shimizu, M.1    Miyake, M.2    Kanke, F.3    Matsumoto, U.4    Shindo, H.5
  • 81
    • 0026532533 scopus 로고
    • Preferential binding of E. coli histone-like protein HU alpha to negatively supercoiled DNA
    • Shindo, H., Furubayashi, A., Shimizu, M., Miyake, M., and Imamoto, F. (1992) Preferential binding of E. coli histone-like protein HU alpha to negatively supercoiled DNA. Nucleic Acids Res 20: 1553-1558.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1553-1558
    • Shindo, H.1    Furubayashi, A.2    Shimizu, M.3    Miyake, M.4    Imamoto, F.5
  • 82
    • 0343240577 scopus 로고
    • Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling
    • Sinden, R.R., and Pettijohn, D.E. (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
  • 83
    • 7244245362 scopus 로고    scopus 로고
    • Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU reveals their ability to form highly stable DNA-protein complexes
    • Skoko, D., Wong, B., Johnson, R.C., and Marko, J.F. (2004) Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU reveals their ability to form highly stable DNA-protein complexes. Biochemistry 43: 13867-13874.
    • (2004) Biochemistry , vol.43 , pp. 13867-13874
    • Skoko, D.1    Wong, B.2    Johnson, R.C.3    Marko, J.F.4
  • 84
    • 0021760528 scopus 로고
    • H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro
    • Spassky, A., Rimsky, S., Garreau, H., and Buc, H. (1984) H1a, 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
  • 85
    • 0026573628 scopus 로고
    • Lethal overproduction of the Escherichia coli nucleoid protein H-NS: Ultramicroscopic and molecular autopsy
    • Spurio, R., Durrenberger, M., Falconi, M., LaTeana, A., Pon, C.L., and Gualerzi, C.O. (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    Durrenberger, M.2    Falconi, M.3    LaTeana, A.4    Pon, C.L.5    Gualerzi, C.O.6
  • 86
    • 1342324028 scopus 로고    scopus 로고
    • IHF and HU: Flexible architects of bent DNA
    • Swinger, K.K., and Rice, P.A. (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
  • 87
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger, K.K., Lemberg, K.M., Zhang, Y., and Rice, P.A. (2003) Flexible DNA bending in HU-DNA 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
  • 88
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Talukder, A.A., Iwata, A., Nishimura, A., Ueda, S., and 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
    • Talukder, A.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 89
    • 0030220837 scopus 로고    scopus 로고
    • Molecular dynamics simulations of small DNA plasmids: Effects of sequence and supercoiling on intramolecular motions
    • Tan, R.K., Sprous, D., and Harvey, S.C. (1996) Molecular dynamics simulations of small DNA plasmids: effects of sequence and supercoiling on intramolecular motions. Biopolymers 39: 259-278.
    • (1996) Biopolymers , vol.39 , pp. 259-278
    • Tan, R.K.1    Sprous, D.2    Harvey, S.C.3
  • 90
    • 0021286693 scopus 로고
    • 3-A resolution structure of a protein with histone-like properties in prokaryotes
    • Tanaka, I., Appelt, K., Dijk, J., White, S.W., and Wilson, K.S. (1984) 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature 310: 376-381.
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 91
    • 0027172958 scopus 로고
    • Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli
    • Tanaka, H., Goshima, N., Kohno, K., Kano, Y., and Imamoto, F. (1993) Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli. J Biochem (Tokyo) 113: 568-572.
    • (1993) J Biochem (Tokyo) , vol.113 , pp. 568-572
    • Tanaka, H.1    Goshima, N.2    Kohno, K.3    Kano, Y.4    Imamoto, F.5
  • 92
    • 0343340048 scopus 로고    scopus 로고
    • Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
    • Tapias, A., Lopez, G., and Ayora, S. (2000) Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA. Nucleic Acids Res 28: 552-559.
    • (2000) Nucleic Acids Res , vol.28 , pp. 552-559
    • Tapias, A.1    Lopez, G.2    Ayora, S.3
  • 93
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to lambda site-specific recombination complexes
    • Thompson, J.F., and Landy, A. (1988) Empirical estimation of protein-induced DNA bending angles: applications to lambda site-specific recombination complexes. Nucleic Acids Res 16: 9687-9705.
    • (1988) Nucleic Acids Res , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 94
    • 0028306747 scopus 로고
    • Evidence for a regulatory function of the histone-like Escherichia coli protein H-NS in ribosomal RNA synthesis
    • Tippner, D., Afflerbach, H., Bradaczek, C., and Wagner, R. (1994) Evidence for a regulatory function of the histone-like Escherichia coli protein H-NS in ribosomal RNA synthesis. Mol Microbiol 11: 589-604.
    • (1994) Mol Microbiol , vol.11 , pp. 589-604
    • Tippner, D.1    Afflerbach, H.2    Bradaczek, C.3    Wagner, R.4
  • 96
    • 0029812751 scopus 로고    scopus 로고
    • Integration host factor alleviates the H-NS-mediated repression of the early promoter of bacteriophage Mu
    • van Ulsen, P., Hillebrand, M., Zulianello, L., van de Putte, P., and Goosen, N. (1996) Integration host factor alleviates the H-NS-mediated repression of the early promoter of bacteriophage Mu. Mol Microbiol 21: 567-578.
    • (1996) Mol Microbiol , vol.21 , pp. 567-578
    • Van Ulsen, P.1    Hillebrand, M.2    Zulianello, L.3    Van De Putte, P.4    Goosen, N.5
  • 99
    • 0028308422 scopus 로고
    • Conformational and thermodynamic properties of supercoiled DNA
    • Vologodskii, A.V., and Cozzarelli, N.R. (1994) Conformational and thermodynamic properties of supercoiled DNA. Annu Rev Biophys Biomol Struct 23: 609-643.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 609-643
    • Vologodskii, A.V.1    Cozzarelli, N.R.2
  • 100
    • 0032160958 scopus 로고    scopus 로고
    • Kinetics of structural changes in superhelical DNA
    • Wedemann, G., Munkel, C., Schoppe, G., and Langowski, J. (1998) Kinetics of structural changes in superhelical DNA. Phys Rev E 58: 3537-3546.
    • (1998) Phys Rev E , vol.58 , pp. 3537-3546
    • Wedemann, G.1    Munkel, C.2    Schoppe, G.3    Langowski, J.4
  • 101
    • 0037452946 scopus 로고    scopus 로고
    • HU binding to bent DNA: A fluorescence resonance energy transfer and anisotropy study
    • Wojtuszewski, K., and Mukerji, I. (2003) HU binding to bent DNA: a fluorescence resonance energy transfer and anisotropy study. Biochemistry 42: 3096-3104.
    • (2003) Biochemistry , vol.42 , pp. 3096-3104
    • Wojtuszewski, K.1    Mukerji, I.2
  • 102
    • 4344645370 scopus 로고    scopus 로고
    • The HU-DNA binding interaction probed with UV resonance Raman spectroscopy: Structural elements of specificity
    • Wojtuszewski, K., and Mukerji, I. (2004) The HU-DNA binding interaction probed with UV resonance Raman spectroscopy: structural elements of specificity. Protein Sci 13: 2416-2428.
    • (2004) Protein Sci , vol.13 , pp. 2416-2428
    • Wojtuszewski, K.1    Mukerji, I.2
  • 103
    • 0036050398 scopus 로고    scopus 로고
    • The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation
    • Woldringh, C.L. (2002) The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation. Mol Microbiol 45: 17-29.
    • (2002) Mol Microbiol , vol.45 , pp. 17-29
    • Woldringh, C.L.1
  • 104
    • 0029093284 scopus 로고
    • Structure and partitioning of bacterial DNA: Determined by a balance of compaction and expansion forces?
    • Woldringh, C.L., Jensen, P.R., and Westerhoff, H.V. (1995) Structure and partitioning of bacterial DNA: determined by a balance of compaction and expansion forces? FEMS Microbiol Lett 131: 235-242.
    • (1995) FEMS Microbiol Lett , vol.131 , pp. 235-242
    • Woldringh, C.L.1    Jensen, P.R.2    Westerhoff, H.V.3
  • 105
    • 0015506478 scopus 로고
    • On the structure of the folded chromosome of Escherichia coli
    • Worcel, A., and 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
  • 106
    • 0024340266 scopus 로고
    • The interaction of E. coli IHF protein with its specific binding sites
    • Yang, C.C., and Nash, H.A. (1989) The interaction of E. coli IHF protein with its specific binding sites. Cell 57: 869-880.
    • (1989) Cell , vol.57 , pp. 869-880
    • Yang, C.C.1    Nash, H.A.2
  • 107
    • 0029561532 scopus 로고
    • Comparison of protein binding to DNA in vivo and in vitro: Defining an effective intracellular target
    • Yang, S.W., and Nash, H.A. (1995) Comparison of protein binding to DNA in vivo and in vitro: defining an effective intracellular target. EMBO J 14: 6292-6300.
    • (1995) EMBO J , vol.14 , pp. 6292-6300
    • Yang, S.W.1    Nash, H.A.2
  • 108
    • 0025939520 scopus 로고
    • The molecular structure of wild-type and a mutant Fis protein: Relationship between mutational changes and recombinational enhancer function or DNA binding
    • Yuan, H.S., Finkel, S.E., Feng, J.A., Kaczor-Grzeskowiak, M., Johnson, R.C., and Dickerson, R.E. (1991) The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding. Proc Natl Acad Sci USA 88: 9558-9562.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9558-9562
    • Yuan, H.S.1    Finkel, S.E.2    Feng, J.A.3    Kaczor-Grzeskowiak, M.4    Johnson, R.C.5    Dickerson, R.E.6
  • 109
    • 4644232611 scopus 로고    scopus 로고
    • Multiple site-specific binding of Fis protein to Escherichia coli nuoA-N Promoter DNA and its impact on DNA topology visualised by means of scanning force microscopy
    • Zhang, J., Zeuner, Y., Kleefeld, A., Unden, G., and Janshoff, A. (2004) Multiple site-specific binding of Fis protein to Escherichia coli nuoA-N Promoter DNA and its impact on DNA topology visualised by means of scanning force microscopy. Chembiochem 5: 1286.
    • (2004) Chembiochem , vol.5 , pp. 1286
    • Zhang, J.1    Zeuner, Y.2    Kleefeld, A.3    Unden, G.4    Janshoff, A.5
  • 110
    • 0030605841 scopus 로고    scopus 로고
    • Macromolecular crowding and the mandatory condensation of DNA in bacteria
    • Zimmerman, S.B., and Murphy, L.D. (1996) Macromolecular crowding and the mandatory condensation of DNA in bacteria. FEBS Lett 390: 245-248.
    • (1996) FEBS Lett , vol.390 , pp. 245-248
    • Zimmerman, S.B.1    Murphy, L.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.