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Volumn 4, Issue 2, 2009, Pages

The HU regulon is composed of genes responding to anaerobiosis, acid stress, high osmolarity and SOS induction

Author keywords

[No Author keywords available]

Indexed keywords

ACIDITY; ANAEROBIC GROWTH; CATABOLISM; CHROMOSOME; ENERGY METABOLISM; ESCHERICHIA COLI; GENE EXPRESSION; GENETIC TRANSCRIPTION; IN VIVO STUDY; NONHUMAN; OPERON; OSMOLARITY; PHENOTYPE; PROTEIN DNA INTERACTION; REGULON;

EID: 84988735230     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0004367     Document Type: Article
Times cited : (142)

References (92)
  • 1
    • 0343794843 scopus 로고
    • Characterization of a novel, low-molecularweight DNA-binding protein from Escherichia coli
    • Rouviere-Yaniv J, Gros F (1975) Characterization of a novel, low-molecularweight DNA-binding protein from Escherichia coli. Proc Natl Acad Sci U S A 72: 3428-3432.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 3428-3432
    • Rouviere-Yaniv, J.1    Gros, F.2
  • 2
    • 0018644060 scopus 로고
    • Native Escherichia coli HU protein is a heterotypic dimer
    • Rouviere-Yaniv J, Kjeldgaard NO (1979) Native Escherichia coli HU protein is a heterotypic dimer. FEBS Lett 106: 297-300.
    • (1979) FEBS Lett , vol.106 , pp. 297-300
    • Rouviere-Yaniv, J.1    Kjeldgaard, N.O.2
  • 3
    • 2142785151 scopus 로고
    • Cyanobacterial DNA-binding protein related to Escherichia coli HU
    • Haselkorn R, Rouviere-Yaniv J (1976) Cyanobacterial DNA-binding protein related to Escherichia coli HU. Proc Natl Acad Sci U S A 73: 1917-1920.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 1917-1920
    • Haselkorn, R.1    Rouviere-Yaniv, J.2
  • 5
    • 0018405881 scopus 로고
    • E. Coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA
    • Rouviere-Yaniv J, Yaniv M, Germond JE (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
  • 6
    • 0023413620 scopus 로고
    • Histonelike proteins of bacteria
    • Drlica K, Rouviere-Yaniv J (1987) Histonelike proteins of bacteria. Microbiol Rev 51: 301-319.
    • (1987) Microbiol Rev , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 7
    • 0030063060 scopus 로고    scopus 로고
    • Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium
    • Oberto J, Rouviere-Yaniv J (1996) Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium. J Bacteriol 178: 293-297.
    • (1996) J Bacteriol , vol.178 , pp. 293-297
    • Oberto, J.1    Rouviere-Yaniv, J.2
  • 8
    • 0031576352 scopus 로고    scopus 로고
    • Variation in HU composition during growth of Escherichia coli: The heterodimer is required for long term survival
    • Claret L, Rouviere-Yaniv J (1997) Variation in HU composition during growth of Escherichia coli: the heterodimer is required for long term survival. J Mol Biol 273: 93-104.
    • (1997) J Mol Biol , vol.273 , pp. 93-104
    • Claret, L.1    Rouviere-Yaniv, J.2
  • 9
    • 0024373965 scopus 로고
    • Multiple defects in Escherichia coli mutants lacking HU protein
    • Huisman O, Faelen M, Girard D, Jaffe A, Toussaint A, et al. (1989) Multiple defects in Escherichia coli mutants lacking HU protein. J Bacteriol 171: 3704-3712.
    • (1989) J Bacteriol , vol.171 , pp. 3704-3712
    • Huisman, O.1    Faelen, M.2    Girard, D.3    Jaffe, A.4    Toussaint, A.5
  • 10
    • 0025853061 scopus 로고
    • Inhibition of cell division in hupA hupB mutant bacteria lacking HU protein
    • Dri AM, Rouviere-Yaniv J, Moreau PL (1991) Inhibition of cell division in hupA hupB mutant bacteria lacking HU protein. J Bacteriol 173: 2852-2863.
    • (1991) J Bacteriol , vol.173 , pp. 2852-2863
    • Dri, A.M.1    Rouviere-Yaniv, J.2    Moreau, P.L.3
  • 11
    • 0029939230 scopus 로고    scopus 로고
    • Cross-talk between topoisomerase I and HU in Escherichia coli
    • Bensaid A, Almeida A, Drlica K, Rouviere-Yaniv J (1996) Cross-talk between topoisomerase I and HU in Escherichia coli. J Mol Biol 256: 292-300.
    • (1996) J Mol Biol , vol.256 , pp. 292-300
    • Bensaid, A.1    Almeida, A.2    Drlica, K.3    Rouviere-Yaniv, J.4
  • 12
    • 0029991026 scopus 로고    scopus 로고
    • Histone-like protein HU and bacterial DNA topology: Suppression of an HU deficiency by gyrase mutations
    • Malik M, Bensaid A, Rouviere-Yaniv J, Drlica K (1996) Histone-like protein HU and bacterial DNA topology: suppression of an HU deficiency by gyrase mutations. J Mol Biol 256: 66-76.
    • (1996) J Mol Biol , vol.256 , pp. 66-76
    • Malik, M.1    Bensaid, A.2    Rouviere-Yaniv, J.3    Drlica, K.4
  • 13
    • 0030971440 scopus 로고    scopus 로고
    • The Bacillus subtilis chromatinassociated protein Hbsu is involved in DNA repair and recombination
    • Fernandez S, Rojo F, Alonso JC (1997) The Bacillus subtilis chromatinassociated protein Hbsu is involved in DNA repair and recombination. Mol Microbiol 23: 1169-1179.
    • (1997) Mol Microbiol , vol.23 , pp. 1169-1179
    • Fernandez, S.1    Rojo, F.2    Alonso, J.C.3
  • 14
    • 0030601787 scopus 로고    scopus 로고
    • Regulation of HU alpha and HU beta by CRP and FIS in Escherichia coli
    • Claret L, Rouviere-Yaniv J (1996) Regulation of HU alpha and HU beta by CRP and FIS in Escherichia coli. J Mol Biol 263: 126-139.
    • (1996) J Mol Biol , vol.263 , pp. 126-139
    • Claret, L.1    Rouviere-Yaniv, J.2
  • 15
    • 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, 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
  • 16
    • 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, et al. (2003) Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure. J Mol Biol 331: 101-121.
    • (2003) J Mol Biol , vol.331 , pp. 101-121
    • Ramstein, J.1    Hervouet, N.2    Coste, F.3    Zelwer, C.4    Oberto, J.5
  • 17
  • 18
    • 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, 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
  • 19
    • 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, 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
  • 20
    • 0029061514 scopus 로고
    • Increased sensitivity to gamma irradiation in bacteria lacking protein HU
    • Boubrik F, Rouviere-Yaniv J (1995) Increased sensitivity to gamma irradiation in bacteria lacking protein HU. Proc Natl Acad Sci U S A 92: 3958-3962.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3958-3962
    • Boubrik, F.1    Rouviere-Yaniv, J.2
  • 21
    • 0031858092 scopus 로고    scopus 로고
    • Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination
    • Li S, Waters R (1998) Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination. J Bacteriol 180: 3750-3756.
    • (1998) J Bacteriol , vol.180 , pp. 3750-3756
    • Li, S.1    Waters, R.2
  • 23
    • 0034416406 scopus 로고    scopus 로고
    • The histone-like protein HU binds specifically to DNA recombination and repair intermediates
    • Kamashev D, 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
  • 24
    • 0028142574 scopus 로고
    • Evidence for involvement of proteins HU and RpoS in transcription of the osmoresponsive proU operon in Escherichia coli
    • Manna D, Gowrishankar J (1994) Evidence for involvement of proteins HU and RpoS in transcription of the osmoresponsive proU operon in Escherichia coli. J Bacteriol 176: 5378-5384.
    • (1994) J Bacteriol , vol.176 , pp. 5378-5384
    • Manna, D.1    Gowrishankar, J.2
  • 25
    • 0036189578 scopus 로고    scopus 로고
    • The histone-like protein HU does not obstruct movement of T7 RNA polymerase in Escherichia coli cells but stimulates its activity
    • Morales P, Rouviere-Yaniv J, Dreyfus M (2002) The histone-like protein HU does not obstruct movement of T7 RNA polymerase in Escherichia coli cells but stimulates its activity. J Bacteriol 184: 1565-1570.
    • (2002) J Bacteriol , vol.184 , pp. 1565-1570
    • Morales, P.1    Rouviere-Yaniv, J.2    Dreyfus, M.3
  • 26
    • 33646079413 scopus 로고    scopus 로고
    • Three-stage regulation of the amphibolic gal operon: From repressosome to GalR-free DNA
    • Semsey S, Virnik K, Adhya S (2006) Three-stage regulation of the amphibolic gal operon: from repressosome to GalR-free DNA. J Mol Biol 358: 355-363.
    • (2006) J Mol Biol , vol.358 , pp. 355-363
    • Semsey, S.1    Virnik, K.2    Adhya, S.3
  • 27
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli
    • Calvo JM, Matthews RG (1994) The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol Rev 58: 466-490.
    • (1994) Microbiol Rev , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.G.2
  • 28
    • 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, 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
  • 29
    • 35549009343 scopus 로고    scopus 로고
    • High-affinity DNA binding sites for H-NS provide a molecular basis for selective silencing within proteobacterial genomes
    • Lang B, Blot N, Bouffartigues E, Buckle M, Geertz M, et al. (2007) High-affinity DNA binding sites for H-NS provide a molecular basis for selective silencing within proteobacterial genomes. Nucleic Acids Res 35: 6330-6337.
    • (2007) Nucleic Acids Res , vol.35 , pp. 6330-6337
    • Lang, B.1    Blot, N.2    Bouffartigues, E.3    Buckle, M.4    Geertz, M.5
  • 30
    • 33750689137 scopus 로고    scopus 로고
    • Lex marks the spot: The virulent side of SOS and a closer look at the LexA regulon
    • Kelley WL (2006) Lex marks the spot: the virulent side of SOS and a closer look at the LexA regulon. Mol Microbiol 62: 1228-1238.
    • (2006) Mol Microbiol , vol.62 , pp. 1228-1238
    • Kelley, W.L.1
  • 31
    • 7444245668 scopus 로고    scopus 로고
    • Identification of the CRP regulon using in vitro and in vivo transcriptional profiling
    • Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004) Identification of the CRP regulon using in vitro and in vivo transcriptional profiling. Nucleic Acids Res 32: 5874-5893.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5874-5893
    • Zheng, D.1    Constantinidou, C.2    Hobman, J.L.3    Minchin, S.D.4
  • 32
    • 31844431848 scopus 로고    scopus 로고
    • The integration host factor (IHF) integrates stationary-phase and virulence gene expression in Salmonella enterica serovar Typhimurium
    • Mangan MW, Lucchini S, Danino V, Croinin TO, Hinton JC, et al. (2006) The integration host factor (IHF) integrates stationary-phase and virulence gene expression in Salmonella enterica serovar Typhimurium. Mol Microbiol 59: 1831-1847.
    • (2006) Mol Microbiol , vol.59 , pp. 1831-1847
    • Mangan, M.W.1    Lucchini, S.2    Danino, V.3    Croinin, T.O.4    Hinton, J.C.5
  • 33
    • 0033976873 scopus 로고    scopus 로고
    • Histone-like protein HU is required for recA gene-dependent DNA repair and SOS induction pathways in UV-irradiated Escherichia coli
    • Miyabe I, Zhang QM, Kano Y, Yonei S (2000) Histone-like protein HU is required for recA gene-dependent DNA repair and SOS induction pathways in UV-irradiated Escherichia coli. Int J Radiat Biol 76: 43-49.
    • (2000) Int J Radiat Biol , vol.76 , pp. 43-49
    • Miyabe, I.1    Zhang, Q.M.2    Kano, Y.3    Yonei, S.4
  • 34
    • 0041335300 scopus 로고    scopus 로고
    • Physiological studies of Escherichia coli strain MG1655: Growth defects and apparent cross-regulation of gene expression
    • Soupene E, van Heeswijk WC, Plumbridge J, Stewart V, Bertenthal D, et al. (2003) Physiological studies of Escherichia coli strain MG1655: growth defects and apparent cross-regulation of gene expression. J Bacteriol 185: 5611-5626.
    • (2003) J Bacteriol , vol.185 , pp. 5611-5626
    • Soupene, E.1    Van Heeswijk, W.C.2    Plumbridge, J.3    Stewart, V.4    Bertenthal, D.5
  • 35
    • 37449005819 scopus 로고    scopus 로고
    • Comparative genomic hybridization detects secondary chromosomal deletions in Escherichia coli K-12 MG1655 mutants and highlights instability in the flhDC region
    • Hobman JL, Patel MD, Hidalgo-Arroyo GA, Cariss SJ, Avison MB, et al. (2007) Comparative genomic hybridization detects secondary chromosomal deletions in Escherichia coli K-12 MG1655 mutants and highlights instability in the flhDC region. J Bacteriol 189: 8786-8792.
    • (2007) J Bacteriol , vol.189 , pp. 8786-8792
    • Hobman, J.L.1    Patel, M.D.2    Hidalgo-Arroyo, G.A.3    Cariss, S.J.4    Avison, M.B.5
  • 36
    • 0036435633 scopus 로고    scopus 로고
    • Microarray analysis of gene expression during bacteriophage T4 infection
    • Luke K, Radek A, Liu X, Campbell J, Uzan M, et al. (2002) Microarray analysis of gene expression during bacteriophage T4 infection. Virology 299: 182-191.
    • (2002) Virology , vol.299 , pp. 182-191
    • Luke, K.1    Radek, A.2    Liu, X.3    Campbell, J.4    Uzan, M.5
  • 39
    • 5144223827 scopus 로고    scopus 로고
    • Stress and survival of aging Escherichia coli rpoS colonies
    • Saint-Ruf C, Taddei F, Matic I (2004) Stress and survival of aging Escherichia coli rpoS colonies. Genetics 168: 541-546.
    • (2004) Genetics , vol.168 , pp. 541-546
    • Saint-Ruf, C.1    Taddei, F.2    Matic, I.3
  • 40
    • 33644873438 scopus 로고    scopus 로고
    • RegulonDB (version 5.0): Escherichia coli K-12 transcriptional regulatory network, operon organization, and growth conditions
    • Salgado H, Gama-Castro S, Peralta-Gil M, Diaz-Peredo E, Sanchez-Solano F, et al. (2006) RegulonDB (version 5.0): Escherichia coli K-12 transcriptional regulatory network, operon organization, and growth conditions. Nucleic Acids Res 34: D394-397.
    • (2006) Nucleic Acids Res , vol.34 , pp. D394-397
    • Salgado, H.1    Gama-Castro, S.2    Peralta-Gil, M.3    Diaz-Peredo, E.4    Sanchez-Solano, F.5
  • 41
    • 27644580858 scopus 로고    scopus 로고
    • Genomic analysis of LexA binding reveals the permissive nature of the Escherichia coli genome and identifies unconventional target sites
    • Wade JT, Reppas NB, Church GM, Struhl K (2005) Genomic analysis of LexA binding reveals the permissive nature of the Escherichia coli genome and identifies unconventional target sites. Genes Dev 19: 2619-2630.
    • (2005) Genes Dev , vol.19 , pp. 2619-2630
    • Wade, J.T.1    Reppas, N.B.2    Church, G.M.3    Struhl, K.4
  • 42
    • 0027765577 scopus 로고
    • An imbalance of HU synthesis induces mucoidy in Escherichia coli
    • Painbeni E, Mouray E, Gottesman S, Rouviere-Yaniv J (1993) An imbalance of HU synthesis induces mucoidy in Escherichia coli. J Mol Biol 234: 1021-1037.
    • (1993) J Mol Biol , vol.234 , pp. 1021-1037
    • Painbeni, E.1    Mouray, E.2    Gottesman, S.3    Rouviere-Yaniv, J.4
  • 43
    • 0020608087 scopus 로고
    • Coupling of DNA replication and cell division: SulB is an allele of ftsZ
    • Lutkenhaus JF (1983) Coupling of DNA replication and cell division: sulB is an allele of ftsZ. J Bacteriol 154: 1339-1346.
    • (1983) J Bacteriol , vol.154 , pp. 1339-1346
    • Lutkenhaus, J.F.1
  • 44
    • 0031720087 scopus 로고    scopus 로고
    • Escherichia coli HU protein suppresses DNA-gyrase-mediated illegitimate recombination and SOS induction
    • Shanado Y, Kato J, Ikeda H (1998) Escherichia coli HU protein suppresses DNA-gyrase-mediated illegitimate recombination and SOS induction. Genes Cells 3: 511-520.
    • (1998) Genes Cells , vol.3 , pp. 511-520
    • Shanado, Y.1    Kato, J.2    Ikeda, H.3
  • 45
    • 0020536519 scopus 로고
    • Proteins required for ultraviolet light and chemical mutagenesis. Identification of the products of the umuC locus of Escherichia coli
    • Elledge SJ, Walker GC (1983) Proteins required for ultraviolet light and chemical mutagenesis. Identification of the products of the umuC locus of Escherichia coli. J Mol Biol 164: 175-192.
    • (1983) J Mol Biol , vol.164 , pp. 175-192
    • Elledge, S.J.1    Walker, G.C.2
  • 47
    • 2642560509 scopus 로고    scopus 로고
    • Analysis of the lambdoid prophage element e14 in the E. Coli K-12 genome
    • Mehta P, Casjens S, Krishnaswamy S (2004) Analysis of the lambdoid prophage element e14 in the E. coli K-12 genome. BMC Microbiol 4: 4.
    • (2004) BMC Microbiol , vol.4 , pp. 4
    • Mehta, P.1    Casjens, S.2    Krishnaswamy, S.3
  • 48
    • 0031576351 scopus 로고    scopus 로고
    • Role of DNA supercoiling and rpoS sigma factor in the osmotic and growth phase-dependent induction of the gene osmE of Escherichia coli K12
    • Conter A, Menchon C, Gutierrez C (1997) Role of DNA supercoiling and rpoS sigma factor in the osmotic and growth phase-dependent induction of the gene osmE of Escherichia coli K12. J Mol Biol 273: 75-83.
    • (1997) J Mol Biol , vol.273 , pp. 75-83
    • Conter, A.1    Menchon, C.2    Gutierrez, C.3
  • 49
    • 0026762504 scopus 로고
    • OsmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli
    • Yim HH, Villarejo M (1992) osmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli. J Bacteriol 174: 3637-3644.
    • (1992) J Bacteriol , vol.174 , pp. 3637-3644
    • Yim, H.H.1    Villarejo, M.2
  • 50
    • 0024025446 scopus 로고
    • Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli
    • Giaever HM, Styrvold OB, Kaasen I, Strom AR (1988) Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. J Bacteriol 170: 2841-2849.
    • (1988) J Bacteriol , vol.170 , pp. 2841-2849
    • Giaever, H.M.1    Styrvold, O.B.2    Kaasen, I.3    Strom, A.R.4
  • 51
    • 18944381780 scopus 로고    scopus 로고
    • Osmotic regulation of the Escherichia coli bdm (biofilm-dependent modulation) gene by the RcsCDB His-Asp phosphorelay
    • Francez-Charlot A, Castanie-Cornet MP, Gutierrez C, Cam K (2005) Osmotic regulation of the Escherichia coli bdm (biofilm-dependent modulation) gene by the RcsCDB His-Asp phosphorelay. J Bacteriol 187: 3873-3877.
    • (2005) J Bacteriol , vol.187 , pp. 3873-3877
    • Francez-Charlot, A.1    Castanie-Cornet, M.P.2    Gutierrez, C.3    Cam, K.4
  • 52
    • 33749602970 scopus 로고    scopus 로고
    • Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli
    • Weber A, Kogl SA, Jung K (2006) Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli. J Bacteriol 188: 7165-7175.
    • (2006) J Bacteriol , vol.188 , pp. 7165-7175
    • Weber, A.1    Kogl, S.A.2    Jung, K.3
  • 53
    • 0037316190 scopus 로고    scopus 로고
    • A microarray-based antibiotic screen identifies a regulatory role for supercoiling in the osmotic stress response of Escherichia coli
    • Cheung KJ, Badarinarayana V, Selinger DW, Janse D, Church GM (2003) A microarray-based antibiotic screen identifies a regulatory role for supercoiling in the osmotic stress response of Escherichia coli. Genome Res 13: 206-215.
    • (2003) Genome Res , vol.13 , pp. 206-215
    • Cheung, K.J.1    Badarinarayana, V.2    Selinger, D.W.3    Janse, D.4    Church, G.M.5
  • 56
    • 9444285788 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: Tales of an amateur acidophile
    • Foster JW (2004) Escherichia coli acid resistance: tales of an amateur acidophile. Nat Rev Microbiol 2: 898-907.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 898-907
    • Foster, J.W.1
  • 57
    • 0036843687 scopus 로고    scopus 로고
    • Escherichia coli gene expression responsive to levels of the response regulator EvgA
    • Masuda N, Church GM (2002) Escherichia coli gene expression responsive to levels of the response regulator EvgA. J Bacteriol 184: 6225-6234.
    • (2002) J Bacteriol , vol.184 , pp. 6225-6234
    • Masuda, N.1    Church, G.M.2
  • 58
    • 14644415527 scopus 로고    scopus 로고
    • Anaerobic regulation of hydrogenase transcription in different bacteria
    • Kovacs AT, Rakhely G, Balogh J, Maroti G, Fulop A, et al. (2005) Anaerobic regulation of hydrogenase transcription in different bacteria. Biochem Soc Trans 33: 36-38.
    • (2005) Biochem Soc Trans , vol.33 , pp. 36-38
    • Kovacs, A.T.1    Rakhely, G.2    Balogh, J.3    Maroti, G.4    Fulop, A.5
  • 59
    • 0030984442 scopus 로고    scopus 로고
    • In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli
    • Georgellis D, Lynch AS, Lin EC (1997) In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli. J Bacteriol 179: 5429-5435.
    • (1997) J Bacteriol , vol.179 , pp. 5429-5435
    • Georgellis, D.1    Lynch, A.S.2    Lin, E.C.3
  • 60
    • 17644381300 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12: Effects of oxygen availability and ArcA
    • Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, et al. (2005) Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA. J Biol Chem 280: 15084-15096.
    • (2005) J Biol Chem , vol.280 , pp. 15084-15096
    • Salmon, K.A.1    Hung, S.P.2    Steffen, N.R.3    Krupp, R.4    Baldi, P.5
  • 61
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera BA, Beinert H, Khoroshilova N, Kennedy MC, Kiley PJ (1996) DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem 271: 2762-2768.
    • (1996) J Biol Chem , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 62
    • 13244289800 scopus 로고    scopus 로고
    • Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function
    • Kang Y, Weber KD, Qiu Y, Kiley PJ, Blattner FR (2005) Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function. J Bacteriol 187: 1135-1160.
    • (2005) J Bacteriol , vol.187 , pp. 1135-1160
    • Kang, Y.1    Weber, K.D.2    Qiu, Y.3    Kiley, P.J.4    Blattner, F.R.5
  • 63
    • 33646184857 scopus 로고    scopus 로고
    • A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth
    • Constantinidou C, Hobman JL, Griffiths L, Patel MD, Penn CW, et al. (2006) A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth. J Biol Chem 281: 4802-4815.
    • (2006) J Biol Chem , vol.281 , pp. 4802-4815
    • Constantinidou, C.1    Hobman, J.L.2    Griffiths, L.3    Patel, M.D.4    Penn, C.W.5
  • 64
    • 0030770469 scopus 로고    scopus 로고
    • Regulation of the ndh gene of Escherichia coli by integration host factor and a novel regulator, Arr
    • Green J, Anjum MF, Guest JR (1997) Regulation of the ndh gene of Escherichia coli by integration host factor and a novel regulator, Arr. Microbiology 143(Pt 9): 2865-2875.
    • (1997) Microbiology , vol.143 , pp. 2865-2875
    • Green, J.1    Anjum, M.F.2    Guest, J.R.3
  • 65
    • 1842529555 scopus 로고    scopus 로고
    • Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling
    • Liu X, De Wulf P (2004) Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling. J Biol Chem 279: 12588-12597.
    • (2004) J Biol Chem , vol.279 , pp. 12588-12597
    • Liu, X.1    De Wulf, P.2
  • 66
    • 0036231561 scopus 로고    scopus 로고
    • Selective expression of the beta-subunit of nucleoid-associated protein HU during cold shock in Escherichia coli
    • Giangrossi M, Giuliodori AM, Gualerzi CO, Pon CL (2002) Selective expression of the beta-subunit of nucleoid-associated protein HU during cold shock in Escherichia coli. Mol Microbiol 44: 205-216.
    • (2002) Mol Microbiol , vol.44 , pp. 205-216
    • Giangrossi, M.1    Giuliodori, A.M.2    Gualerzi, C.O.3    Pon, C.L.4
  • 67
    • 38649127865 scopus 로고    scopus 로고
    • Reduced apo-fumarate nitrate reductase regulator (apoFNR) as the major form of FNR in aerobically growing Escherichia coli
    • Reinhart F, Achebach S, Koch T, Unden G (2008) Reduced apo-fumarate nitrate reductase regulator (apoFNR) as the major form of FNR in aerobically growing Escherichia coli. J Bacteriol 190: 879-886.
    • (2008) J Bacteriol , vol.190 , pp. 879-886
    • Reinhart, F.1    Achebach, S.2    Koch, T.3    Unden, G.4
  • 68
    • 0025777765 scopus 로고
    • Bacterial DNA supercoiling and [ATP]/[ADP]. Changes associated with a transition to anaerobic growth
    • Hsieh LS, Burger RM, Drlica K (1991) Bacterial DNA supercoiling and [ATP]/[ADP]. Changes associated with a transition to anaerobic growth. J Mol Biol 219: 443-450.
    • (1991) J Mol Biol , vol.219 , pp. 443-450
    • Hsieh, L.S.1    Burger, R.M.2    Drlica, K.3
  • 69
    • 34248370213 scopus 로고    scopus 로고
    • Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling
    • Guo F, Adhya S (2007) Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling. Proc Natl Acad Sci U S A 104: 4309-4314.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4309-4314
    • Guo, F.1    Adhya, S.2
  • 70
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger KK, Lemberg KM, Zhang Y, Rice PA (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
  • 71
    • 33845796196 scopus 로고    scopus 로고
    • Structure-based analysis of HU-DNA binding
    • Swinger KK, Rice PA (2007) Structure-based analysis of HU-DNA binding. J Mol Biol 365: 1005-1016.
    • (2007) J Mol Biol , vol.365 , pp. 1005-1016
    • Swinger, K.K.1    Rice, P.A.2
  • 72
    • 33745612978 scopus 로고    scopus 로고
    • Homeostatic regulation of supercoiling sensitivity coordinates transcription of the bacterial genome
    • Blot N, Mavathur R, Geertz M, Travers A, Muskhelishvili G (2006) Homeostatic regulation of supercoiling sensitivity coordinates transcription of the bacterial genome. EMBO Rep 7: 710-715.
    • (2006) EMBO Rep , vol.7 , pp. 710-715
    • Blot, N.1    Mavathur, R.2    Geertz, M.3    Travers, A.4    Muskhelishvili, G.5
  • 73
    • 11344266685 scopus 로고    scopus 로고
    • Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli
    • Peter BJ, Arsuaga J, Breier AM, Khodursky AB, Brown PO, et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol 5: R87.
    • (2004) Genome Biol , vol.5 , pp. R87
    • Peter, B.J.1    Arsuaga, J.2    Breier, A.M.3    Khodursky, A.B.4    Brown, P.O.5
  • 74
    • 0023117639 scopus 로고
    • Use of site-specific recombination as a probe of DNA structure and metabolism in vivo
    • Bliska JB, Cozzarelli NR (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.B.1    Cozzarelli, N.R.2
  • 75
    • 33846659467 scopus 로고    scopus 로고
    • Transcription factor distribution in Escherichia coli: Studies with FNR protein
    • Grainger DC, Aiba H, Hurd D, Browning DF, Busby SJ (2007) Transcription factor distribution in Escherichia coli: studies with FNR protein. Nucleic Acids Res 35: 269-278.
    • (2007) Nucleic Acids Res , vol.35 , pp. 269-278
    • Grainger, D.C.1    Aiba, H.2    Hurd, D.3    Browning, D.F.4    Busby, S.J.5
  • 77
    • 0027741294 scopus 로고
    • Altered topoisomerase activities may be involved in the regulation of DNA supercoiling in aerobic-anaerobic transitions in Escherichia coli
    • Cortassa S, Aon MA (1993) Altered topoisomerase activities may be involved in the regulation of DNA supercoiling in aerobic-anaerobic transitions in Escherichia coli. Mol Cell Biochem 126: 115-124.
    • (1993) Mol Cell Biochem , vol.126 , pp. 115-124
    • Cortassa, S.1    Aon, M.A.2
  • 78
    • 0017629285 scopus 로고
    • Localization of the HU protein on the Escherichia coli nucleoid
    • Rouviere-Yaniv J (1978) Localization of the HU protein on the Escherichia coli nucleoid. Cold Spring Harb Symp Quant Biol 42 Pt 1: 439-447.
    • (1978) Cold Spring Harb Symp Quant Biol , vol.42 , pp. 439-447
    • Rouviere-Yaniv, J.1
  • 79
    • 0026019440 scopus 로고
    • HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments
    • Bonnefoy E, Rouviere-Yaniv J (1991) HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments. EMBO J 10: 687-696.
    • (1991) EMBO J , vol.10 , pp. 687-696
    • Bonnefoy, E.1    Rouviere-Yaniv, J.2
  • 80
    • 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 U S A 78: 224-228.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 224-228
    • Sinden, R.R.1    Pettijohn, D.E.2
  • 81
    • 84865249128 scopus 로고    scopus 로고
    • Regulation of transcription in bacteria by DNA supercoiling
    • Berlin Heidelberg: Springer-Verlag
    • Dorman CJ (2008) Regulation of Transcription in Bacteria by DNA Supercoiling. Bacterial Physiology: A Molecular Approach. Berlin Heidelberg: Springer-Verlag. pp 151-176.
    • (2008) Bacterial Physiology: A Molecular Approach , pp. 151-176
    • Dorman, C.J.1
  • 83
    • 3342959174 scopus 로고    scopus 로고
    • Modulation of DNA conformations through the formation of alternative high-order HUDNA complexes
    • Sagi D, Friedman N, Vorgias C, Oppenheim AB, Stavans J (2004) Modulation of DNA conformations through the formation of alternative high-order HUDNA 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
  • 86
    • 38849099823 scopus 로고    scopus 로고
    • BAGET: A web server for the effortless retrieval of prokaryotic gene context and sequence
    • Oberto J (2008) BAGET: a web server for the effortless retrieval of prokaryotic gene context and sequence. Bioinformatics 24: 424-425.
    • (2008) Bioinformatics , vol.24 , pp. 424-425
    • Oberto, J.1
  • 87
    • 0023255472 scopus 로고
    • Improved single and multicopy lacbased cloning vectors for protein and operon fusions
    • Simons RW, Houman F, Kleckner N (1987) Improved single and multicopy lacbased cloning vectors for protein and operon fusions. Gene 53: 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 89
    • 2342634096 scopus 로고    scopus 로고
    • DNA-Chip Analyser (dChip)
    • Parmigiani G, Garrett ES, Irizarry R, Zeger SL, eds. New York: Springer
    • Li C, Wong WH (2003) DNA-Chip Analyser (dChip). In: Parmigiani G, Garrett ES, Irizarry R, Zeger SL, eds. The analysis of gene expression data: methods and software. New York: Springer. pp 120-141.
    • (2003) The Analysis of Gene Expression Data: Methods and Software , pp. 120-141
    • Li, C.1    Wong, W.H.2
  • 90
    • 9444225935 scopus 로고    scopus 로고
    • Java Treeview-extensible visualization of microarray data
    • Saldanha AJ (2004) Java Treeview-extensible visualization of microarray data. Bioinformatics 20: 3246-3248.
    • (2004) Bioinformatics , vol.20 , pp. 3246-3248
    • Saldanha, A.J.1
  • 91
    • 33645511192 scopus 로고    scopus 로고
    • StataCorp, College Station Texas: Statacorp LP
    • StataCorp (2005) Stata Statistical Software: Release 9. College Station Texas: Statacorp LP.
    • (2005) Stata Statistical Software: Release 9


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