메뉴 건너뛰기




Volumn 10, Issue 3, 2014, Pages

Bacterial Regulon Evolution: Distinct Responses and Roles for the Identical OmpR Proteins of Salmonella Typhimurium and Escherichia coli in the Acid Stress Response

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; MESSENGER RNA; OUTER MEMBRANE PROTEIN REGULATOR; BACTERIAL PROTEIN; OSMOLARITY RESPONSE REGULATOR PROTEINS; TRANSACTIVATOR PROTEIN;

EID: 84897451640     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004215     Document Type: Article
Times cited : (85)

References (88)
  • 1
    • 67650601963 scopus 로고    scopus 로고
    • Evolution of transcriptional regulatory circuits in bacteria
    • Perez JC, Groisman EA, (2009) Evolution of transcriptional regulatory circuits in bacteria. Cell 138: 233-244.
    • (2009) Cell , vol.138 , pp. 233-244
    • Perez, J.C.1    Groisman, E.A.2
  • 2
    • 43749083945 scopus 로고    scopus 로고
    • Amino acids important for DNA recognition by the response regulator OmpR
    • Rhee JE, Sheng W, Morgan LK, Nolet R, Liao X, et al. (2008) Amino acids important for DNA recognition by the response regulator OmpR. J Biol Chem 13: 8664-8677.
    • (2008) J Biol Chem , vol.13 , pp. 8664-8677
    • Rhee, J.E.1    Sheng, W.2    Morgan, L.K.3    Nolet, R.4    Liao, X.5
  • 3
    • 84859235790 scopus 로고    scopus 로고
    • A fundamental regulatory mechanism operating through OmpR and DNA topology controls expression of Salmonella Pathogenicity islands SPI-1 and SPI-2
    • Cameron ADS, Dorman CJ, (2012) A fundamental regulatory mechanism operating through OmpR and DNA topology controls expression of Salmonella Pathogenicity islands SPI-1 and SPI-2. PLoS Genet 3: e1002615.
    • (2012) PLoS Genet , vol.3
    • Cameron, A.D.S.1    Dorman, C.J.2
  • 4
    • 0027382142 scopus 로고
    • The influence of DNA topology on the environmental regulation of a pH-regulated locus in Salmonella Typhimurium
    • Karem K, Foster JW, (1993) The influence of DNA topology on the environmental regulation of a pH-regulated locus in Salmonella Typhimurium. Mol Microbiol 10: 75-86.
    • (1993) Mol Microbiol , vol.10 , pp. 75-86
    • Karem, K.1    Foster, J.W.2
  • 5
    • 0004738888 scopus 로고
    • Regulation of bacterial DNA supercoiling: plasmid linking numbers vary with growth temperature
    • Goldstein E, Drlica K, (1984) Regulation of bacterial DNA supercoiling: plasmid linking numbers vary with growth temperature. Proc Natl Acad Sci USA 81: 4046-4050.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4046-4050
    • Goldstein, E.1    Drlica, K.2
  • 6
    • 0024024835 scopus 로고
    • DNA supercoiling and the anaerobic and growth phase regulation of tonB gene expression
    • Dorman CJ, Barr GC, Ní Bhriain N, Higgins CF, (1988) DNA supercoiling and the anaerobic and growth phase regulation of tonB gene expression. J Bacteriol 170: 2816-2826.
    • (1988) J Bacteriol , vol.170 , pp. 2816-2826
    • Dorman, C.J.1    Barr, G.C.2    Ní Bhriain, N.3    Higgins, C.F.4
  • 7
    • 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
  • 8
    • 0025915548 scopus 로고
    • Bacterial DNA supercoiling and [ATP]/[ADP] ratio: changes associated with salt shock
    • Hsieh LS, Rouvière-Yaniv J, Drlica K, (1991) Bacterial DNA supercoiling and [ATP]/[ADP] ratio: changes associated with salt shock. J Bacteriol 173: 3914-3917.
    • (1991) J Bacteriol , vol.173 , pp. 3914-3917
    • Hsieh, L.S.1    Rouvière-Yaniv, J.2    Drlica, K.3
  • 9
    • 0025140705 scopus 로고
    • Signal transduction and gene regulation through the phosphorylation of two regulatory components: the molecular basis for the osmotic regulation of the porin genes
    • Mizuno T, Mizushima S, (1990) Signal transduction and gene regulation through the phosphorylation of two regulatory components: the molecular basis for the osmotic regulation of the porin genes. Mol Microbiol 7: 1077-1082.
    • (1990) Mol Microbiol , vol.7 , pp. 1077-1082
    • Mizuno, T.1    Mizushima, S.2
  • 10
    • 0001427734 scopus 로고
    • In: Hoch J, Silhavy TJ editors. Washington, DC: American Society for Microbiology Press
    • Pratt L, Silhavy TJ, (1995) In: Hoch J, Silhavy TJ editors. Two-component signal transduction. Washington, DC: American Society for Microbiology Press. pp 105-107.
    • (1995) Two-component signal transduction , pp. 105-107
    • Pratt, L.1    Silhavy, T.J.2
  • 11
    • 0028289709 scopus 로고
    • Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli
    • Roberts DL, Bennett DW, Forst SA, (1994) Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli. J Biol Chem 269: 8728-8733.
    • (1994) J Biol Chem , vol.269 , pp. 8728-8733
    • Roberts, D.L.1    Bennett, D.W.2    Forst, S.A.3
  • 12
    • 0031568318 scopus 로고    scopus 로고
    • The DNA binding domain of OmpR: crystal structures of a winged helix transcription factor
    • Martinez-Hackeret E, Stock AM, (1997) The DNA binding domain of OmpR: crystal structures of a winged helix transcription factor. Structure 5: 109-124.
    • (1997) Structure , vol.5 , pp. 109-124
    • Martinez-Hackeret, E.1    Stock, A.M.2
  • 13
    • 0027771353 scopus 로고
    • Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coli
    • Delgado J, Forst S, Harlocker S, Inouye M, (1993) Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coli. Mol Microbiol 5: 1037-1047.
    • (1993) Mol Microbiol , vol.5 , pp. 1037-1047
    • Delgado, J.1    Forst, S.2    Harlocker, S.3    Inouye, M.4
  • 14
    • 0017522339 scopus 로고
    • Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli
    • Alphen WV, Lugtenberg B, (1977) Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J Bacteriol 131: 623-630.
    • (1977) J Bacteriol , vol.131 , pp. 623-630
    • Alphen, W.V.1    Lugtenberg, B.2
  • 15
    • 0017650936 scopus 로고
    • Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coli K-12
    • Sarma V, Reeves P, (1977) Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coli K-12. J Bacteriol 132: 23-27.
    • (1977) J Bacteriol , vol.132 , pp. 23-27
    • Sarma, V.1    Reeves, P.2
  • 16
    • 0023864296 scopus 로고
    • EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12
    • Slauch JM, Garrett S, Jackson DE, Silhavy TJ, (1988) EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12. J Bacteriol 170: 439-441.
    • (1988) J Bacteriol , vol.170 , pp. 439-441
    • Slauch, J.M.1    Garrett, S.2    Jackson, D.E.3    Silhavy, T.J.4
  • 17
    • 84861849986 scopus 로고    scopus 로고
    • The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm
    • Wang LC, Morgan LK, Godakumbura P, Kenney LJ, Anand GS, (2012) The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm. EMBO J 11: 2648-59.
    • (2012) EMBO J , vol.11 , pp. 2648-2659
    • Wang, L.C.1    Morgan, L.K.2    Godakumbura, P.3    Kenney, L.J.4    Anand, G.S.5
  • 18
    • 0026498184 scopus 로고
    • Salmonella Typhimurium activates virulence gene transcription within acidified macrophage phagosomes
    • Alpuche-Aranda CM, Swanson JA, Loomis WP, Miller SI, (1992) Salmonella Typhimurium activates virulence gene transcription within acidified macrophage phagosomes. Proc Natl Acad Sci USA 89: 10079-10083.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10079-10083
    • Alpuche-Aranda, C.M.1    Swanson, J.A.2    Loomis, W.P.3    Miller, S.I.4
  • 19
    • 0029994912 scopus 로고    scopus 로고
    • Acidification of phagosomes containing Salmonella Typhimurium in murine macrophages
    • Rathman M, Sjaastad MD, Falkow S, (1996) Acidification of phagosomes containing Salmonella Typhimurium in murine macrophages. Infect Immun 64: 2765-2773.
    • (1996) Infect Immun , vol.64 , pp. 2765-2773
    • Rathman, M.1    Sjaastad, M.D.2    Falkow, S.3
  • 21
    • 0028324804 scopus 로고
    • Acid and base resistance in Escherichia coli and Shigella flexneri: Role of rpoS and growth pH
    • Small P, Blankenhorn D, Welty D, Zinser E, Slonczewski JL, (1994) Acid and base resistance in Escherichia coli and Shigella flexneri: Role of rpoS and growth pH. J Bacteriol 176: 1729-1737.
    • (1994) J Bacteriol , vol.176 , pp. 1729-1737
    • Small, P.1    Blankenhorn, D.2    Welty, D.3    Zinser, E.4    Slonczewski, J.L.5
  • 22
    • 0029073161 scopus 로고
    • Comparative analysis of extreme acid survival in Salmonella Typhimurium, Shigella flexneri and Escherichia coli
    • Lin J, Lee IS, Frey J, Slonczewski JL, Foster JW, (1995) Comparative analysis of extreme acid survival in Salmonella Typhimurium, Shigella flexneri and Escherichia coli. J Bacteriol 177: 4097-4104.
    • (1995) J Bacteriol , vol.177 , pp. 4097-4104
    • Lin, J.1    Lee, I.S.2    Frey, J.3    Slonczewski, J.L.4    Foster, J.W.5
  • 23
    • 0024399678 scopus 로고
    • Characterization of porin and ompR mutants of a virulent strain of Salmonella Typhimurium: ompR mutants are attenuated in vivo
    • Dorman CJ, Chatfield S, Higgins CF, Hayward C, Dougan G, (1989) Characterization of porin and ompR mutants of a virulent strain of Salmonella Typhimurium: ompR mutants are attenuated in vivo. Infect Immun 57: 2136-2140.
    • (1989) Infect Immun , vol.57 , pp. 2136-2140
    • Dorman, C.J.1    Chatfield, S.2    Higgins, C.F.3    Hayward, C.4    Dougan, G.5
  • 24
    • 0029817221 scopus 로고    scopus 로고
    • Identification of a pathogenicity island required for Salmonella survival in host cells
    • Ochman H, Soncini FC, Solomon F, Groisman EA, (1996) Identification of a pathogenicity island required for Salmonella survival in host cells. Proc Natl Acad Sci USA 15: 7800-7804.
    • (1996) Proc Natl Acad Sci USA , vol.15 , pp. 7800-7804
    • Ochman, H.1    Soncini, F.C.2    Solomon, F.3    Groisman, E.A.4
  • 25
    • 0029852315 scopus 로고    scopus 로고
    • Distribution of pathogenicity islands in Salmonella spp
    • Ochman H, Groisman EA, (1996) Distribution of pathogenicity islands in Salmonella spp. Infect Immun 12: 5410-5412.
    • (1996) Infect Immun , vol.12 , pp. 5410-5412
    • Ochman, H.1    Groisman, E.A.2
  • 26
    • 0029913901 scopus 로고    scopus 로고
    • Identification of a virulence locus encoding a second type III secretion system in Salmonella Typhimurium
    • Shea JE, Hensel M, Gleeson C, Holden DW, (1996) Identification of a virulence locus encoding a second type III secretion system in Salmonella Typhimurium. Proc Natl Acad Sci USA 93: 2593-2597.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2593-2597
    • Shea, J.E.1    Hensel, M.2    Gleeson, C.3    Holden, D.W.4
  • 27
    • 13844255187 scopus 로고    scopus 로고
    • Hierarchical gene regulators adapt Salmonella Typhimurium to its host milieus
    • Rhen M, Dorman CJ, (2005) Hierarchical gene regulators adapt Salmonella Typhimurium to its host milieus. Int J Med Microbiol 294: 487-502.
    • (2005) Int J Med Microbiol , vol.294 , pp. 487-502
    • Rhen, M.1    Dorman, C.J.2
  • 28
    • 0033954447 scopus 로고    scopus 로고
    • OmpR regulates the two-component system SsrA-SsrB in Salmonella pathogenicity island 2
    • Lee AK, Detweiler CS, Falkow S, (2000) OmpR regulates the two-component system SsrA-SsrB in Salmonella pathogenicity island 2. J Bacteriol 182: 771-781.
    • (2000) J Bacteriol , vol.182 , pp. 771-781
    • Lee, A.K.1    Detweiler, C.S.2    Falkow, S.3
  • 29
    • 84897465405 scopus 로고    scopus 로고
    • Dual regulation by phospho-OmpR of ssrA/B gene expression in Salmonella pathogenicity island 2
    • Feng X, Oropeza R, Kenney LJ, (2003) Dual regulation by phospho-OmpR of ssrA/B gene expression in Salmonella pathogenicity island 2. Mol Microbiol 1: 231-247.
    • (2003) Mol Microbiol , vol.1 , pp. 231-247
    • Feng, X.1    Oropeza, R.2    Kenney, L.J.3
  • 30
    • 63749110404 scopus 로고    scopus 로고
    • Control of Salmonella pathogenicity island-2 gene expression
    • Fass E, Groisman EA, (2009) Control of Salmonella pathogenicity island-2 gene expression. Curr Opin Microbiol 12: 199-204.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 199-204
    • Fass, E.1    Groisman, E.A.2
  • 31
    • 33749988005 scopus 로고    scopus 로고
    • Roles for DNA supercoiling and the Fis protein in modulation expression of virulence genes during intracellular growth of Salmonella enterica serovar Typhimurium
    • Ó Cróinín T, Carroll RK, Kelly A, Dorman CJ, (2006) Roles for DNA supercoiling and the Fis protein in modulation expression of virulence genes during intracellular growth of Salmonella enterica serovar Typhimurium. Mol Microbiol 62: 869-882.
    • (2006) Mol Microbiol , vol.62 , pp. 869-882
    • Ó Cróinín, T.1    Carroll, R.K.2    Kelly, A.3    Dorman, C.J.4
  • 32
    • 0343729469 scopus 로고    scopus 로고
    • OmpR regulates the stationary-phase acid tolerance response of Salmonella enterica serovar Typhimurium
    • Bang IS, Kim BH, Foster JW, Park YK, (2000) OmpR regulates the stationary-phase acid tolerance response of Salmonella enterica serovar Typhimurium. J Bacteriol 182: 2245-2252.
    • (2000) J Bacteriol , vol.182 , pp. 2245-2252
    • Bang, I.S.1    Kim, B.H.2    Foster, J.W.3    Park, Y.K.4
  • 33
    • 0036015640 scopus 로고    scopus 로고
    • Autoinduction of the ompR response regulator by acid shock and control of the Salmonella typhimurium acid tolerance response
    • Bang IS, Audia JP, Park YK, Foster JW, (2002) Autoinduction of the ompR response regulator by acid shock and control of the Salmonella typhimurium acid tolerance response. Mol Microbiol 44: 1235-1250.
    • (2002) Mol Microbiol , vol.44 , pp. 1235-1250
    • Bang, I.S.1    Audia, J.P.2    Park, Y.K.3    Foster, J.W.4
  • 34
    • 0345434969 scopus 로고    scopus 로고
    • The ompB operon partially determines differential expression of OmpC in Salmonella Typhi and Escherichia coli
    • Martinez-Flores I, Cano R, Bustamante VH, Calva E, Puente JL, (1999) The ompB operon partially determines differential expression of OmpC in Salmonella Typhi and Escherichia coli. J Bacteriol 2: 556-562.
    • (1999) J Bacteriol , vol.2 , pp. 556-562
    • Martinez-Flores, I.1    Cano, R.2    Bustamante, V.H.3    Calva, E.4    Puente, J.L.5
  • 35
    • 0023821284 scopus 로고
    • Structure and expression of the ompB operon, the regulatory locus for the outer membrane porin regulon in Salmonella Typhimurium LT-2
    • Liljestrom P, Laamanen I, Palva ET, (1988) Structure and expression of the ompB operon, the regulatory locus for the outer membrane porin regulon in Salmonella Typhimurium LT-2. J Mol Biol 201: 663-673.
    • (1988) J Mol Biol , vol.201 , pp. 663-673
    • Liljestrom, P.1    Laamanen, I.2    Palva, E.T.3
  • 36
    • 0025939651 scopus 로고
    • Integration host factor binds specifically to multiple sites in the ompB promoter of Escherichia coli and inhibits transcription
    • Tsui P, Huang L, Freundlich M, (1991) Integration host factor binds specifically to multiple sites in the ompB promoter of Escherichia coli and inhibits transcription. J Bacteriol 173: 5800-5807.
    • (1991) J Bacteriol , vol.173 , pp. 5800-5807
    • Tsui, P.1    Huang, L.2    Freundlich, M.3
  • 37
    • 0028325749 scopus 로고
    • A distant upstream site involved in the negative regulation of the Escherichia coli ompF gene
    • Huang KJ, Schieberl JL, Igo MM, (1994) A distant upstream site involved in the negative regulation of the Escherichia coli ompF gene. J Bacteriol 5: 1309-1315.
    • (1994) J Bacteriol , vol.5 , pp. 1309-1315
    • Huang, K.J.1    Schieberl, J.L.2    Igo, M.M.3
  • 39
    • 0036303447 scopus 로고    scopus 로고
    • A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC
    • Mattison K, Oropeza R, Byers N, Kenney LJ, (2002) A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC. J Mol Biol 4: 497-511.
    • (2002) J Mol Biol , vol.4 , pp. 497-511
    • Mattison, K.1    Oropeza, R.2    Byers, N.3    Kenney, L.J.4
  • 40
    • 0029153682 scopus 로고
    • Molecular analysis of OmpR binding sequences involved in the regulation of ompF in Escherichia coli
    • Forst S, Kalve I, Durski W, (1995) Molecular analysis of OmpR binding sequences involved in the regulation of ompF in Escherichia coli. FEMS Microbiol Lett 2: 147-15.
    • (1995) FEMS Microbiol Lett , vol.2 , pp. 115-147
    • Forst, S.1    Kalve, I.2    Durski, W.3
  • 41
    • 0028875660 scopus 로고
    • Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli
    • Harlocker SL, Bergstrom L, Inouye M, (1995) Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli. J Biol Chem 45: 26849-26856.
    • (1995) J Biol Chem , vol.45 , pp. 26849-26856
    • Harlocker, S.L.1    Bergstrom, L.2    Inouye, M.3
  • 42
    • 33745219470 scopus 로고    scopus 로고
    • Transcription regulation of ompF and ompC by a single transcription factor, OmpR
    • Yoshida T, Qin L, Egger LA, Inouye M, (2006) Transcription regulation of ompF and ompC by a single transcription factor, OmpR. J Biol Chem 25: 17114-17123.
    • (2006) J Biol Chem , vol.25 , pp. 17114-17123
    • Yoshida, T.1    Qin, L.2    Egger, L.A.3    Inouye, M.4
  • 43
    • 0023272277 scopus 로고
    • OmpR and EnvZ are pleiotropic regulatory proteins: positive regulation of the tripeptide permease (tppB) of Salmonella Typhimurium
    • Gibson MM, Ellis EM, Graeme-Cook KA, Higgins CF, (1987) OmpR and EnvZ are pleiotropic regulatory proteins: positive regulation of the tripeptide permease (tppB) of Salmonella Typhimurium. Mol Gen Genet 1: 120-129.
    • (1987) Mol Gen Genet , vol.1 , pp. 120-129
    • Gibson, M.M.1    Ellis, E.M.2    Graeme-Cook, K.A.3    Higgins, C.F.4
  • 44
    • 2942552241 scopus 로고    scopus 로고
    • The Escherichia coli tppB (ydgR) gene represents a new class of OmpR-regulated genes
    • Goh EB, Siino DF, Igo MM, (2004) The Escherichia coli tppB (ydgR) gene represents a new class of OmpR-regulated genes. J Bacteriol 12: 4019-4024.
    • (2004) J Bacteriol , vol.12 , pp. 4019-4024
    • Goh, E.B.1    Siino, D.F.2    Igo, M.M.3
  • 45
    • 0031932327 scopus 로고    scopus 로고
    • Curli fibers are highly conserved between Salmonella Typhimurium and Escherichia coli with respect to operon structure and regulation
    • Romling U, Bian Z, Hammar M, Sierralta WD, Normark S, (1998) Curli fibers are highly conserved between Salmonella Typhimurium and Escherichia coli with respect to operon structure and regulation. J Bacteriol 3: 722-731.
    • (1998) J Bacteriol , vol.3 , pp. 722-731
    • Romling, U.1    Bian, Z.2    Hammar, M.3    Sierralta, W.D.4    Normark, S.5
  • 46
    • 0043166926 scopus 로고    scopus 로고
    • Complex regulation of csgD promoter activity by global regulatory proteins
    • Gerstel U, Park C, Romling U, (2003) Complex regulation of csgD promoter activity by global regulatory proteins. Mol Microbiol 3: 639-654.
    • (2003) Mol Microbiol , vol.3 , pp. 639-654
    • Gerstel, U.1    Park, C.2    Romling, U.3
  • 47
    • 0035205423 scopus 로고    scopus 로고
    • Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene
    • Prigent-Combaret C, Brombacher E, Vidal O, Ambert A, Lejeune P, et al. (2001) Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene. J Bacteriol 24: 7213-7223.
    • (2001) J Bacteriol , vol.24 , pp. 7213-7223
    • Prigent-Combaret, C.1    Brombacher, E.2    Vidal, O.3    Ambert, A.4    Lejeune, P.5
  • 48
    • 0029130181 scopus 로고
    • Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR
    • Shin S, Park C, (1995) Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR. J Bacteriol 16: 4696-4702.
    • (1995) J Bacteriol , vol.16 , pp. 4696-4702
    • Shin, S.1    Park, C.2
  • 49
    • 33645066654 scopus 로고    scopus 로고
    • Remodelling of the Escherichia coli outer membrane by two small regulatory RNAs
    • Guillier M, Gottesman S, (2006) Remodelling of the Escherichia coli outer membrane by two small regulatory RNAs. Mol Microbiol 1: 231-247.
    • (2006) Mol Microbiol , vol.1 , pp. 231-247
    • Guillier, M.1    Gottesman, S.2
  • 50
    • 68249102779 scopus 로고    scopus 로고
    • A strand-specific RNA-Seq analysis of the transcriptome of the typhoid bacillus Salmonella Typhi
    • Perkins TT, Kingsley RA, Fookes MC, Gardner PP, James KD, et al. (2009) A strand-specific RNA-Seq analysis of the transcriptome of the typhoid bacillus Salmonella Typhi. PLoS Genet 7: e1000569.
    • (2009) PLoS Genet , vol.7
    • Perkins, T.T.1    Kingsley, R.A.2    Fookes, M.C.3    Gardner, P.P.4    James, K.D.5
  • 51
    • 0029812095 scopus 로고    scopus 로고
    • Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine
    • Neely MN, Olson ER, (1996) Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine. J Bacteriol 178: 5522-5528.
    • (1996) J Bacteriol , vol.178 , pp. 5522-5528
    • Neely, M.N.1    Olson, E.R.2
  • 52
    • 0022574417 scopus 로고
    • Streptococcal cytoplasmic pH is regulated by changes in amount and activity of a proton-translocating ATPase
    • Kobayashi H, Suzuki T, Unemoto T, (1986) Streptococcal cytoplasmic pH is regulated by changes in amount and activity of a proton-translocating ATPase. J Biol Chem 261: 627-630.
    • (1986) J Biol Chem , vol.261 , pp. 627-630
    • Kobayashi, H.1    Suzuki, T.2    Unemoto, T.3
  • 53
    • 33744950278 scopus 로고    scopus 로고
    • Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli
    • Douchin V, Bohn C, Bouloc P, (2006) Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli. J Biol Chem 18: 12253-12259.
    • (2006) J Biol Chem , vol.18 , pp. 12253-12259
    • Douchin, V.1    Bohn, C.2    Bouloc, P.3
  • 54
    • 0036386339 scopus 로고    scopus 로고
    • Interaction of the atypical prokaryotic transcription activator FlhD2C2 with early promoters of the flagellar gene hierarchy
    • Claret L, Hughes C, (2002) Interaction of the atypical prokaryotic transcription activator FlhD2C2 with early promoters of the flagellar gene hierarchy. J Mol Biol 2: 185-199.
    • (2002) J Mol Biol , vol.2 , pp. 185-199
    • Claret, L.1    Hughes, C.2
  • 55
    • 0036068774 scopus 로고    scopus 로고
    • LrhA as a new transcriptional key regulator of flagella, motility and chemotaxis genes in Escherichia coli
    • Lehnen D, Blumer C, Polen T, Wackwitz B, Wendisch VF, et al. (2002) LrhA as a new transcriptional key regulator of flagella, motility and chemotaxis genes in Escherichia coli. Mol Microbiol 2: 521-532.
    • (2002) Mol Microbiol , vol.2 , pp. 521-532
    • Lehnen, D.1    Blumer, C.2    Polen, T.3    Wackwitz, B.4    Wendisch, V.F.5
  • 56
    • 27144443126 scopus 로고    scopus 로고
    • Regulation of type 1 fimbriae synthesis and biofilm formation by the transcriptional regulator LrhA of Escherichia coli
    • Blumer C, Kleefeld A, Lehnen D, Heintz M, Dobrindt, et al, (2005) Regulation of type 1 fimbriae synthesis and biofilm formation by the transcriptional regulator LrhA of Escherichia coli. Microbiology 10: 3287-3298.
    • (2005) Microbiology , vol.10 , pp. 3287-3298
    • Blumer, C.1    Kleefeld, A.2    Lehnen, D.3    Heintz, M.4    Dobrindt5
  • 57
    • 78049444220 scopus 로고    scopus 로고
    • Escherichia coli K-12 possesses multiple cryptic but functional chaperone-usher fimbriae with distinct surface specificities
    • Korea CG, Badouraly R, Prevost MC, Ghigo JM, Beloin C, (2010) Escherichia coli K-12 possesses multiple cryptic but functional chaperone-usher fimbriae with distinct surface specificities. Environ microbiol 7: 1957-1977.
    • (2010) Environ Microbiol , vol.7 , pp. 1957-1977
    • Korea, C.G.1    Badouraly, R.2    Prevost, M.C.3    Ghigo, J.M.4    Beloin, C.5
  • 58
    • 0026759317 scopus 로고
    • The regulation of expression of the porin gene ompC by acid pH
    • Thomas AD, Booth IR, (1992) The regulation of expression of the porin gene ompC by acid pH. J Gen Microbiol 9: 1829-35.
    • (1992) J Gen Microbiol , vol.9 , pp. 1829-1835
    • Thomas, A.D.1    Booth, I.R.2
  • 59
    • 77952858676 scopus 로고    scopus 로고
    • pH sensing by intracellular Salmonella induces effector translocation
    • Yu XJ, McGourty K, Liu M, Unsworth KE, Holden DW, (2010) pH sensing by intracellular Salmonella induces effector translocation. Science 5981: 1040-3.
    • (2010) Science , vol.5981 , pp. 1040-1043
    • Yu, X.J.1    McGourty, K.2    Liu, M.3    Unsworth, K.E.4    Holden, D.W.5
  • 60
    • 0029416946 scopus 로고
    • hilA is a novel ompR/toxR family member that activates the expression of Salmonella Typhimurium invasion genes
    • Bajaj V, Hwang C, Lee CA, (1995) hilA is a novel ompR/toxR family member that activates the expression of Salmonella Typhimurium invasion genes. Mol Microbiol 4: 715-727.
    • (1995) Mol Microbiol , vol.4 , pp. 715-727
    • Bajaj, V.1    Hwang, C.2    Lee, C.A.3
  • 61
    • 22644442538 scopus 로고    scopus 로고
    • HilD, HilC and RtsA constitute a feed forward loop that controls expression of the SPI1 type three secretion system regulator hilA in Salmonella enterica serovar Typhimurium
    • Ellermeier CD, Ellermeier JR, Slauch JM, (2005) HilD, HilC and RtsA constitute a feed forward loop that controls expression of the SPI1 type three secretion system regulator hilA in Salmonella enterica serovar Typhimurium. Mol Microbiol 3: 691-705.
    • (2005) Mol Microbiol , vol.3 , pp. 691-705
    • Ellermeier, C.D.1    Ellermeier, J.R.2    Slauch, J.M.3
  • 62
    • 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 MD, Carroll RK, Danino V, Hinton JC, et al. (2004) A global role for Fis in the transcriptional control of metabolism and type III secretion in Salmonella enterica serovar Typhimurium. Microbiology 7: 2037-2053.
    • (2004) Microbiology , vol.7 , pp. 2037-2053
    • Kelly, A.1    Goldberg, M.D.2    Carroll, R.K.3    Danino, V.4    Hinton, J.C.5
  • 64
    • 77952820341 scopus 로고    scopus 로고
    • Genome-wide analysis of the H-NS and Sfh regulatory networks in Salmonella Typhimurium identifies a plasmid-encoded transcription silencing mechanism
    • Dillon SC, Cameron AD, Hokamp K, Lucchini S, Hinton JC, et al. (2010) Genome-wide analysis of the H-NS and Sfh regulatory networks in Salmonella Typhimurium identifies a plasmid-encoded transcription silencing mechanism. Mol Microbiol 5: 1250-1265.
    • (2010) Mol Microbiol , vol.5 , pp. 1250-1265
    • Dillon, S.C.1    Cameron, A.D.2    Hokamp, K.3    Lucchini, S.4    Hinton, J.C.5
  • 65
    • 79959574265 scopus 로고    scopus 로고
    • Transcriptional priming of Salmonella pathogenicity Island-2 precedes cellular invasion
    • Osborne SE, Coombes BK, (2011) Transcriptional priming of Salmonella pathogenicity Island-2 precedes cellular invasion. PloS One 6: e21648.
    • (2011) PloS One , vol.6
    • Osborne, S.E.1    Coombes, B.K.2
  • 66
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella Typhimurium type III protein secretion system
    • Kubori T, Matsushima Y, Nakamura D, Uralil J, Lara-Tejero M, et al. (1998) Supramolecular structure of the Salmonella Typhimurium type III protein secretion system. Science 5363: 602-605.
    • (1998) Science , vol.5363 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3    Uralil, J.4    Lara-Tejero, M.5
  • 67
    • 7644229970 scopus 로고    scopus 로고
    • The response regulator SsrB activates transcription and binds to a region overlapping OmpR binding sites at Salmonella pathogenicity island 2
    • Feng X, Walthers D, Oropeza R, Kenney LJ, (2004) The response regulator SsrB activates transcription and binds to a region overlapping OmpR binding sites at Salmonella pathogenicity island 2. Mol Microbiol 54: 823-835.
    • (2004) Mol Microbiol , vol.54 , pp. 823-835
    • Feng, X.1    Walthers, D.2    Oropeza, R.3    Kenney, L.J.4
  • 68
    • 34447321831 scopus 로고    scopus 로고
    • The response regulator SsrB activates expression of diverse Salmonella pathogenicity island 2 promoters and counters silencing by the nucleoid-associated protein H-NS
    • Walthers D, Carroll RK, Navarre WW, Libby SJ, Fang FC, et al. (2007) The response regulator SsrB activates expression of diverse Salmonella pathogenicity island 2 promoters and counters silencing by the nucleoid-associated protein H-NS. Mol Microbiol 2: 477-493.
    • (2007) Mol Microbiol , vol.2 , pp. 477-493
    • Walthers, D.1    Carroll, R.K.2    Navarre, W.W.3    Libby, S.J.4    Fang, F.C.5
  • 69
    • 77950441670 scopus 로고    scopus 로고
    • Identification of the regulatory logic controlling Salmonella pathoadaptation by the SsrA-SsrB two-component system
    • Tomljenovic-Berube AM, Mulder DT, Whiteside MD, Brinkman FS, Coombes BK, (2010) Identification of the regulatory logic controlling Salmonella pathoadaptation by the SsrA-SsrB two-component system. PLoS Genet 3: e1000875.
    • (2010) PLoS Genet , vol.3
    • Tomljenovic-Berube, A.M.1    Mulder, D.T.2    Whiteside, M.D.3    Brinkman, F.S.4    Coombes, B.K.5
  • 70
    • 34250739997 scopus 로고    scopus 로고
    • Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system
    • Gerlach RG, Jäckel D, Stecher B, Wagner C, Lupas A, et al. (2007) Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system. Cell Microbiol 9: 1834-1850.
    • (2007) Cell Microbiol , vol.9 , pp. 1834-1850
    • Gerlach, R.G.1    Jäckel, D.2    Stecher, B.3    Wagner, C.4    Lupas, A.5
  • 71
    • 79960431243 scopus 로고    scopus 로고
    • Functional dissection of SiiE, a giant non-fimbrial adhesin of Salmonella Typhimurium
    • Wagner C, Polke M, Gerlach RG, Linke D, Stierhof YD, et al. (2011) Functional dissection of SiiE, a giant non-fimbrial adhesin of Salmonella Typhimurium. Cell Microbiol 13: 1286-1301.
    • (2011) Cell Microbiol , vol.13 , pp. 1286-1301
    • Wagner, C.1    Polke, M.2    Gerlach, R.G.3    Linke, D.4    Stierhof, Y.D.5
  • 72
    • 79953059399 scopus 로고    scopus 로고
    • DNA supercoiling is differentially regulated by environmental factors and FIS in Escherichia coli and Salmonella Typhimurium
    • Cameron AD, Stoebel DM, Dorman CJ, (2011) DNA supercoiling is differentially regulated by environmental factors and FIS in Escherichia coli and Salmonella Typhimurium. Mol Microbiol 80: 85-101.
    • (2011) Mol Microbiol , vol.80 , pp. 85-101
    • Cameron, A.D.1    Stoebel, D.M.2    Dorman, C.J.3
  • 73
    • 0017043747 scopus 로고
    • Novobiocin and coumermycin inhibit DNA supercoiling catalyzed by DNA gyrase
    • Gellert M, O'Dea MH, Itoh T, Tomizawa J, (1976) Novobiocin and coumermycin inhibit DNA supercoiling catalyzed by DNA gyrase. Proc Natl Acad Sci USA 12: 4474-4478.
    • (1976) Proc Natl Acad Sci USA , vol.12 , pp. 4474-4478
    • Gellert, M.1    O'Dea, M.H.2    Itoh, T.3    Tomizawa, J.4
  • 74
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman EA, (2001) The pleiotropic two-component regulatory system PhoP-PhoQ. J Bacteriol 6: 1835-1842.
    • (2001) J Bacteriol , vol.6 , pp. 1835-1842
    • Groisman, E.A.1
  • 75
    • 84879919792 scopus 로고    scopus 로고
    • A bacterial virulence protein promotes pathogenicity by inhibiting the bacterium's own F1Fo ATP synthase
    • Lee E-J, Pontes MH, Groisman EA, (2013) A bacterial virulence protein promotes pathogenicity by inhibiting the bacterium's own F1Fo ATP synthase. Cell 154: 146-156.
    • (2013) Cell , vol.154 , pp. 146-156
    • Lee, E.-J.1    Pontes, M.H.2    Groisman, E.A.3
  • 76
    • 0030865142 scopus 로고    scopus 로고
    • The Salmonella selC locus contains a pathogenicity island mediating intramacrophage survival
    • Blanc-Potard AB, Groisman EA, (1997) The Salmonella selC locus contains a pathogenicity island mediating intramacrophage survival. EMBO J 17: 5376-5385.
    • (1997) EMBO J , vol.17 , pp. 5376-5385
    • Blanc-Potard, A.B.1    Groisman, E.A.2
  • 77
    • 0036267390 scopus 로고    scopus 로고
    • mig-14 is a Salmonella gene that plays a role in bacterial resistance to antimicrobial peptides
    • Brodsky IE, Ernst RK, Miller SI, Falkow S, (2002) mig-14 is a Salmonella gene that plays a role in bacterial resistance to antimicrobial peptides. J Bacteriol 184: 3203-3213.
    • (2002) J Bacteriol , vol.184 , pp. 3203-3213
    • Brodsky, I.E.1    Ernst, R.K.2    Miller, S.I.3    Falkow, S.4
  • 78
    • 84876543942 scopus 로고    scopus 로고
    • RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more
    • (Database issue)
    • Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L,et al. (2013) RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more. Nucleic Acids Res 41 (Database issue): D203-213.
    • (2013) Nucleic Acids Res , vol.41 , pp. 203-213
    • Salgado, H.1    Peralta-Gil, M.2    Gama-Castro, S.3    Santos-Zavaleta, A.4    Muñiz-Rascado, L.5
  • 79
    • 67849122320 scopus 로고    scopus 로고
    • MEME SUITE: tools for motif discovery and searching
    • (Web Server issue)
    • Bailey TL, Boden M, Buske FA, Frith M, Grant CE,et al. (2009) MEME SUITE: tools for motif discovery and searching. Nucleic Acids Res 37 (Web Server issue): W202-208.
    • (2009) Nucleic Acids Res , vol.37 , pp. 202-208
    • Bailey, T.L.1    Boden, M.2    Buske, F.A.3    Frith, M.4    Grant, C.E.5
  • 80
    • 52749097035 scopus 로고    scopus 로고
    • Using RSAT to scan genome sequences for transcription factor binding sites and cis-regulatory modules
    • Turatsinze JV, Thomas-Chollier M, Defrance M, (2008) van Helden J, (2008) Using RSAT to scan genome sequences for transcription factor binding sites and cis-regulatory modules. Nature protocols 10: 1578-1588.
    • (2008) Nature Protocols , vol.10 , pp. 1578-1588
    • Turatsinze, J.V.1    Thomas-Chollier, M.2    Defrance, M.3    van Helden, J.4
  • 81
    • 80053189299 scopus 로고    scopus 로고
    • A systems biology approach sheds new light on Escherichia coli acid resistance
    • Stincone A, Daudi N, Rathman AS, Antczak P, Henderson I, et al. (2011) A systems biology approach sheds new light on Escherichia coli acid resistance. Nucleic Acids Res 39: 7512-7528.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7512-7528
    • Stincone, A.1    Daudi, N.2    Rathman, A.S.3    Antczak, P.4    Henderson, I.5
  • 82
    • 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
  • 84
    • 70350686719 scopus 로고    scopus 로고
    • The role of DNA shape in protein-DNA recognition
    • Rohs R, West SM, Sosinsky A, Liu P Mann RS, et al. (2009) The role of DNA shape in protein-DNA recognition. Nature. 461: 1248-53.
    • (2009) Nature , vol.461 , pp. 1248-1253
    • Rohs, R.1    West, S.M.2    Sosinsky, A.3    Liu, P.4    Mann, R.S.5
  • 85
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel HJ, Bonner DM, (1956) Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem 1: 97-106.
    • (1956) J Biol Chem , vol.1 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 86
    • 60649103647 scopus 로고    scopus 로고
    • Acid stress activation of the sigma(E) stress response in Salmonella enterica serovar Typhimurium
    • Muller C, Bang IS, Velayudhan J, Karlinsey J, Papenfort K, et al. (2009) Acid stress activation of the sigma(E) stress response in Salmonella enterica serovar Typhimurium. Mol Microbiol 71: 1228-1238.
    • (2009) Mol Microbiol , vol.71 , pp. 1228-1238
    • Muller, C.1    Bang, I.S.2    Velayudhan, J.3    Karlinsey, J.4    Papenfort, K.5
  • 87
    • 65649152564 scopus 로고    scopus 로고
    • A green fluorescent protein (GFP)-based plasmid system to study post-transcriptional control of gene expression in vivo
    • Urban JH, Vogel J, (2009) A green fluorescent protein (GFP)-based plasmid system to study post-transcriptional control of gene expression in vivo. Methods Mol Biol 540: 301-319.
    • (2009) Methods Mol Biol , vol.540 , pp. 301-319
    • Urban, J.H.1    Vogel, J.2
  • 88
    • 31344436263 scopus 로고    scopus 로고
    • ChIPOTle: a user-friendly tool for the analysis of ChIP-chip data
    • Buck MJ, Nobel AB, Lieb JD, (2005) ChIPOTle: a user-friendly tool for the analysis of ChIP-chip data. Genome Biol 6: R97.
    • (2005) Genome Biol , vol.6
    • Buck, M.J.1    Nobel, A.B.2    Lieb, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.