메뉴 건너뛰기




Volumn 23, Issue , 2015, Pages 8-13

Integrated circuits: How transcriptional silencing and counter-silencing facilitate bacterial evolution

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; CURVED DNA; DNA BINDING PROTEIN; H NS NUCLEOPROTEIN; NUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 84910091088     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2014.10.005     Document Type: Review
Times cited : (52)

References (76)
  • 1
    • 0030870440 scopus 로고    scopus 로고
    • How Salmonella became a pathogen
    • Groisman E.A., Ochman H. How Salmonella became a pathogen. Trends Microbiol 1997, 5:343-349.
    • (1997) Trends Microbiol , vol.5 , pp. 343-349
    • Groisman, E.A.1    Ochman, H.2
  • 2
    • 0030606233 scopus 로고    scopus 로고
    • Pathogenicity islands: bacterial evolution in quantum leaps
    • Groisman E.A., Ochman H. Pathogenicity islands: bacterial evolution in quantum leaps. Cell 1996, 87:791-794.
    • (1996) Cell , vol.87 , pp. 791-794
    • Groisman, E.A.1    Ochman, H.2
  • 3
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • Ochman H., Lawrence J.G., Groisman E.A. Lateral gene transfer and the nature of bacterial innovation. Nature 2000, 405:299-304.
    • (2000) Nature , vol.405 , pp. 299-304
    • Ochman, H.1    Lawrence, J.G.2    Groisman, E.A.3
  • 4
    • 0026596979 scopus 로고
    • Horizontal transfer of a phosphatase gene as evidence for mosaic structure of the Salmonella genome
    • Groisman E.A., Saier M.H.J., Ochman H. Horizontal transfer of a phosphatase gene as evidence for mosaic structure of the Salmonella genome. EMBO J 1992, 11:1309-1316.
    • (1992) EMBO J , vol.11 , pp. 1309-1316
    • Groisman, E.A.1    Saier, M.H.J.2    Ochman, H.3
  • 5
    • 33746008173 scopus 로고    scopus 로고
    • Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella
    • Navarre W.W., Porwollik S., Wang Y., McClelland M., Rosen H., Libby S.J., Fang F.C. Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella. Science 2006, 313:236-238.
    • (2006) Science , vol.313 , pp. 236-238
    • Navarre, W.W.1    Porwollik, S.2    Wang, Y.3    McClelland, M.4    Rosen, H.5    Libby, S.J.6    Fang, F.C.7
  • 7
    • 34250724903 scopus 로고    scopus 로고
    • Silencing of xenogeneic DNA by H-NS-facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA
    • Navarre W.W., McClelland M., Libby S.J., Fang F.C. Silencing of xenogeneic DNA by H-NS-facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA. Genes Dev 2007, 21:1456-1471.
    • (2007) Genes Dev , vol.21 , pp. 1456-1471
    • Navarre, W.W.1    McClelland, M.2    Libby, S.J.3    Fang, F.C.4
  • 9
    • 0035083932 scopus 로고    scopus 로고
    • H-NS and H-NS-like proteins in Gram-negative bacteria and their multiple role in the regulation of bacterial metabolism
    • Bertin P., Hommais F., Krin E., Soutourina O., Tendeng C., Derzelle S., Danchin A. H-NS and H-NS-like proteins in Gram-negative bacteria and their multiple role in the regulation of bacterial metabolism. Biochimie 2001, 83:235-241.
    • (2001) Biochimie , vol.83 , pp. 235-241
    • Bertin, P.1    Hommais, F.2    Krin, E.3    Soutourina, O.4    Tendeng, C.5    Derzelle, S.6    Danchin, A.7
  • 10
    • 0344118072 scopus 로고    scopus 로고
    • MvaT proteins in Pseudomonas spp.: a novel class of H-NS-like proteins
    • Tendeng C., Soutourina O.A., Danchin A., Bertin P.N. MvaT proteins in Pseudomonas spp.: a novel class of H-NS-like proteins. Microbiology 2003, 149:3047-3050.
    • (2003) Microbiology , vol.149 , pp. 3047-3050
    • Tendeng, C.1    Soutourina, O.A.2    Danchin, A.3    Bertin, P.N.4
  • 11
    • 57749113200 scopus 로고    scopus 로고
    • H-NS family members function coordinately in an opportunistic pathogen
    • Castang S., McManus H.R., Turner K.H., Dove S.L. H-NS family members function coordinately in an opportunistic pathogen. Proc Natl Acad Sci U S A 2008, 105:18947-18952.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18947-18952
    • Castang, S.1    McManus, H.R.2    Turner, K.H.3    Dove, S.L.4
  • 12
    • 55749090843 scopus 로고    scopus 로고
    • Lsr2 of Mycobacterium represents a novel class of H-NS-like proteins
    • Gordon B.R., Imperial R., Wang L., Navarre W.W., Liu J. Lsr2 of Mycobacterium represents a novel class of H-NS-like proteins. J Bacteriol 2008, 190:7052-7059.
    • (2008) J Bacteriol , vol.190 , pp. 7052-7059
    • Gordon, B.R.1    Imperial, R.2    Wang, L.3    Navarre, W.W.4    Liu, J.5
  • 16
    • 77951072446 scopus 로고    scopus 로고
    • Bending and compaction of DNA by proteins
    • RSC Press, P.A. Rice, C.C. Correll (Eds.)
    • Johnson R.C., Stella S., Heiss J.K. Bending and compaction of DNA by proteins. Protein-Nucleic Acid Interactions 2008, 176-220. RSC Press. P.A. Rice, C.C. Correll (Eds.).
    • (2008) Protein-Nucleic Acid Interactions , pp. 176-220
    • Johnson, R.C.1    Stella, S.2    Heiss, J.K.3
  • 18
    • 0030976054 scopus 로고    scopus 로고
    • The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending
    • Spurio R., Falconi M., Brandi A., Pon C.L., Gualerzi C.O. The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J 1997, 16:1795-1805.
    • (1997) EMBO J , vol.16 , pp. 1795-1805
    • Spurio, R.1    Falconi, M.2    Brandi, A.3    Pon, C.L.4    Gualerzi, C.O.5
  • 19
    • 84867500676 scopus 로고    scopus 로고
    • Higher order oligomerization is required for H-NS family member MvaT to form gene-silencing nucleoprotein filament
    • Winardhi R.S., Fu W., Castang S., Li Y., Dove S.L., Yan J. Higher order oligomerization is required for H-NS family member MvaT to form gene-silencing nucleoprotein filament. Nucleic Acids Res 2012, 40:8942-8952.
    • (2012) Nucleic Acids Res , vol.40 , pp. 8942-8952
    • Winardhi, R.S.1    Fu, W.2    Castang, S.3    Li, Y.4    Dove, S.L.5    Yan, J.6
  • 22
    • 78349236998 scopus 로고    scopus 로고
    • High-order oligomerization is required for the function of the H-NS family member MvaT in Pseudomonas aeruginosa
    • Castang S., Dove S.L. High-order oligomerization is required for the function of the H-NS family member MvaT in Pseudomonas aeruginosa. Mol Microbiol 2010, 78:916-931.
    • (2010) Mol Microbiol , vol.78 , pp. 916-931
    • Castang, S.1    Dove, S.L.2
  • 23
    • 84862175853 scopus 로고    scopus 로고
    • The structure of the oligomerization domain of Lsr2 from Mycobacterium tuberculosis reveals a mechanism for chromosome organization and protection
    • Summers E.L., Meindl K., Uson I., Mitra A.K., Radjainia M., Colangeli R., Alland D., Arcus V.L. The structure of the oligomerization domain of Lsr2 from Mycobacterium tuberculosis reveals a mechanism for chromosome organization and protection. PLoS ONE 2012, 7:e38542.
    • (2012) PLoS ONE , vol.7 , pp. e38542
    • Summers, E.L.1    Meindl, K.2    Uson, I.3    Mitra, A.K.4    Radjainia, M.5    Colangeli, R.6    Alland, D.7    Arcus, V.L.8
  • 24
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame R.T., Wyman C., Goosen N. H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res 2000, 28:3504-3510.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 25
    • 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., Goosen N. Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1. J Biol Chem 2002, 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
  • 27
    • 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., Wagner R. The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex. J Mol Biol 2000, 298:737-748.
    • (2000) J Mol Biol , vol.298 , pp. 737-748
    • Schroder, O.1    Wagner, R.2
  • 28
    • 25844463677 scopus 로고    scopus 로고
    • DNA looping-mediated repression by histone-like protein H-NS: specific requirement of Esigma70 as a cofactor for looping
    • Shin M., Song M., Rhee J.H., Hong Y., Kim Y.J., Seok Y.J., Ha K.S., Jung S.H., Choy H.E. DNA looping-mediated repression by histone-like protein H-NS: specific requirement of Esigma70 as a cofactor for looping. Genes Dev 2005, 19:2388-2398.
    • (2005) Genes Dev , vol.19 , pp. 2388-2398
    • Shin, M.1    Song, M.2    Rhee, J.H.3    Hong, Y.4    Kim, Y.J.5    Seok, Y.J.6    Ha, K.S.7    Jung, S.H.8    Choy, H.E.9
  • 29
    • 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., Stavans J. Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor. Biophys J 2003, 84:2467-2473.
    • (2003) Biophys J , vol.84 , pp. 2467-2473
    • Amit, R.1    Oppenheim, A.B.2    Stavans, J.3
  • 30
    • 76749118994 scopus 로고    scopus 로고
    • A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes
    • Liu Y., Chen H., Kenney L.J., Yan J. A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes. Genes Dev 2010, 24:339-344.
    • (2010) Genes Dev , vol.24 , pp. 339-344
    • Liu, Y.1    Chen, H.2    Kenney, L.J.3    Yan, J.4
  • 32
    • 84878554539 scopus 로고    scopus 로고
    • Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2
    • Qu Y., Lim C.J., Whang Y.R., Liu J., Yan J. Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2. Nucleic Acids Res 2013, 41:5263-5272.
    • (2013) Nucleic Acids Res , vol.41 , pp. 5263-5272
    • Qu, Y.1    Lim, C.J.2    Whang, Y.R.3    Liu, J.4    Yan, J.5
  • 33
    • 84864150307 scopus 로고    scopus 로고
    • Nucleoprotein filament formation is the structural basis for bacterial protein H-NS gene silencing
    • Lim C.J., Lee S.Y., Kenney L.J., Yan J. Nucleoprotein filament formation is the structural basis for bacterial protein H-NS gene silencing. Sci Rep 2012, 2:509.
    • (2012) Sci Rep , vol.2 , pp. 509
    • Lim, C.J.1    Lee, S.Y.2    Kenney, L.J.3    Yan, J.4
  • 35
    • 53449102029 scopus 로고    scopus 로고
    • Anti-silencing: overcoming H-NS-mediated repression of transcription in Gram-negative enteric bacteria
    • Stoebel D.M., Free A., Dorman C.J. Anti-silencing: overcoming H-NS-mediated repression of transcription in Gram-negative enteric bacteria. Microbiology 2008, 154:2533-2545.
    • (2008) Microbiology , vol.154 , pp. 2533-2545
    • Stoebel, D.M.1    Free, A.2    Dorman, C.J.3
  • 36
    • 0024601077 scopus 로고
    • A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells
    • Fields P.I., Groisman E.A., Heffron F. A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells. Science 1989, 243:1059-1062.
    • (1989) Science , vol.243 , pp. 1059-1062
    • Fields, P.I.1    Groisman, E.A.2    Heffron, F.3
  • 37
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence
    • Miller S.I., Kukral A.M., Mekalanos J.J. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc Natl Acad Sci U S A 1989, 86:5054-5058.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 38
    • 0029671310 scopus 로고    scopus 로고
    • Mg2+ as an extracellular signal: environmental regulation of Salmonella virulence
    • Garcia Vescovi E., Soncini F.C., Groisman E.A. Mg2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 1996, 84:165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 41
    • 84910042947 scopus 로고    scopus 로고
    • Evolutionary expansion of a regulatory network by counter-silencing
    • Will W.R., Bale D.H., Reid P.J., Libby S.J., Fang F.C. Evolutionary expansion of a regulatory network by counter-silencing. Nat Commun 2014, 5:5270.
    • (2014) Nat Commun , vol.5 , pp. 5270
    • Will, W.R.1    Bale, D.H.2    Reid, P.J.3    Libby, S.J.4    Fang, F.C.5
  • 42
    • 84859951838 scopus 로고    scopus 로고
    • The promoter architectural landscape of the Salmonella PhoP regulon
    • Zwir I., Latifi T., Perez J.C., Huang H., Groisman E.A. The promoter architectural landscape of the Salmonella PhoP regulon. Mol Microbiol 2012, 84:463-485.
    • (2012) Mol Microbiol , vol.84 , pp. 463-485
    • Zwir, I.1    Latifi, T.2    Perez, J.C.3    Huang, H.4    Groisman, E.A.5
  • 44
    • 67650601963 scopus 로고    scopus 로고
    • Evolution of transcriptional regulatory circuits in bacteria
    • Perez J.C., Groisman E.A. Evolution of transcriptional regulatory circuits in bacteria. Cell 2009, 138:233-244.
    • (2009) Cell , vol.138 , pp. 233-244
    • Perez, J.C.1    Groisman, E.A.2
  • 45
    • 80052774659 scopus 로고    scopus 로고
    • The structure of a transcription activation subcomplex reveals how sigma(70) is recruited to PhoB promoters
    • Blanco A.G., Canals A., Bernues J., Sola M., Coll M. The structure of a transcription activation subcomplex reveals how sigma(70) is recruited to PhoB promoters. EMBO J 2011, 30:3776-3785.
    • (2011) EMBO J , vol.30 , pp. 3776-3785
    • Blanco, A.G.1    Canals, A.2    Bernues, J.3    Sola, M.4    Coll, M.5
  • 46
    • 84887308033 scopus 로고    scopus 로고
    • The bacterial response regulator ArcA uses a diverse binding site architecture to regulate carbon oxidation globally
    • Park D.M., Akhtar M.S., Ansari A.Z., Landick R., Kiley P.J. The bacterial response regulator ArcA uses a diverse binding site architecture to regulate carbon oxidation globally. PLoS Genet 2013, 9:e1003839.
    • (2013) PLoS Genet , vol.9 , pp. e1003839
    • Park, D.M.1    Akhtar, M.S.2    Ansari, A.Z.3    Landick, R.4    Kiley, P.J.5
  • 47
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price N.L., Raivio T.L. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J Bacteriol 2009, 191:1798-1815.
    • (2009) J Bacteriol , vol.191 , pp. 1798-1815
    • Price, N.L.1    Raivio, T.L.2
  • 48
    • 36249017917 scopus 로고    scopus 로고
    • Programming gene expression with combinatorial promoters
    • Cox R.S., Surette M.G., Elowitz M.B. Programming gene expression with combinatorial promoters. Mol Syst Biol 2007, 3:145.
    • (2007) Mol Syst Biol , vol.3 , pp. 145
    • Cox, R.S.1    Surette, M.G.2    Elowitz, M.B.3
  • 49
    • 0032509098 scopus 로고    scopus 로고
    • Lac and lambda repressors relieve silencing of the Escherichia coli bgl promoter. Activation by alteration of a repressing nucleoprotein complex
    • Caramel A., Schnetz K. Lac and lambda repressors relieve silencing of the Escherichia coli bgl promoter. Activation by alteration of a repressing nucleoprotein complex. J Mol Biol 1998, 284:875-883.
    • (1998) J Mol Biol , vol.284 , pp. 875-883
    • Caramel, A.1    Schnetz, K.2
  • 50
    • 80055064471 scopus 로고    scopus 로고
    • Rational design of an artificial genetic switch: co-option of the H-NS-repressed proU operon by the VirB virulence master regulator
    • Kane K.A., Dorman C.J. Rational design of an artificial genetic switch: co-option of the H-NS-repressed proU operon by the VirB virulence master regulator. J Bacteriol 2011, 193:5950-5960.
    • (2011) J Bacteriol , vol.193 , pp. 5950-5960
    • Kane, K.A.1    Dorman, C.J.2
  • 51
    • 84890352725 scopus 로고    scopus 로고
    • Structural insights into VirB-DNA complexes reveal mechanism of transcriptional activation of virulence genes
    • Gao X., Zou T., Mu Z., Qin B., Yang J., Waltersperger S., Wang M., Cui S., Jin Q. Structural insights into VirB-DNA complexes reveal mechanism of transcriptional activation of virulence genes. Nucleic Acids Res 2013, 41:10529-10541.
    • (2013) Nucleic Acids Res , vol.41 , pp. 10529-10541
    • Gao, X.1    Zou, T.2    Mu, Z.3    Qin, B.4    Yang, J.5    Waltersperger, S.6    Wang, M.7    Cui, S.8    Jin, Q.9
  • 52
    • 84866024286 scopus 로고    scopus 로고
    • LeuO is a global regulator of gene expression in Salmonella enterica serovar Typhimurium
    • Dillon S.C., Espinosa E., Hokamp K., Ussery D.W., Casadesus J., Dorman C.J. LeuO is a global regulator of gene expression in Salmonella enterica serovar Typhimurium. Mol Microbiol 2012, 85:1072-1089.
    • (2012) Mol Microbiol , vol.85 , pp. 1072-1089
    • Dillon, S.C.1    Espinosa, E.2    Hokamp, K.3    Ussery, D.W.4    Casadesus, J.5    Dorman, C.J.6
  • 53
    • 80053951751 scopus 로고    scopus 로고
    • Novel roles of LeuO in transcription regulation of E. coli genome: antagonistic interplay with the universal silencer H-NS
    • Shimada T., Bridier A., Briandet R., Ishihama A. Novel roles of LeuO in transcription regulation of E. coli genome: antagonistic interplay with the universal silencer H-NS. Mol Microbiol 2011, 82:378-397.
    • (2011) Mol Microbiol , vol.82 , pp. 378-397
    • Shimada, T.1    Bridier, A.2    Briandet, R.3    Ishihama, A.4
  • 55
    • 17644392863 scopus 로고    scopus 로고
    • LeuO protein delimits the transcriptionally active and repressive domains on the bacterial chromosome
    • Chen C.C., Wu H.Y. LeuO protein delimits the transcriptionally active and repressive domains on the bacterial chromosome. J Biol Chem 2005, 280:15111-15121.
    • (2005) J Biol Chem , vol.280 , pp. 15111-15121
    • Chen, C.C.1    Wu, H.Y.2
  • 56
    • 84901236472 scopus 로고    scopus 로고
    • The Salmonella enterica serovar Typhi LeuO global regulator forms tetramers: residues involved in oligomerization. DNA binding, and transcriptional regulation
    • Guadarrama C., Medrano-Lopez A., Oropeza R., Hernandez-Lucas I., Calva E. The Salmonella enterica serovar Typhi LeuO global regulator forms tetramers: residues involved in oligomerization. DNA binding, and transcriptional regulation. J Bacteriol 2014, 196:2143-2154.
    • (2014) J Bacteriol , vol.196 , pp. 2143-2154
    • Guadarrama, C.1    Medrano-Lopez, A.2    Oropeza, R.3    Hernandez-Lucas, I.4    Calva, E.5
  • 57
    • 0037013282 scopus 로고    scopus 로고
    • Molecular dissection of VirB, a key regulator of the virulence cascade of Shigella flexneri
    • Beloin C., McKenna S., Dorman C.J. Molecular dissection of VirB, a key regulator of the virulence cascade of Shigella flexneri. J Biol Chem 2002, 277:15333-15344.
    • (2002) J Biol Chem , vol.277 , pp. 15333-15344
    • Beloin, C.1    McKenna, S.2    Dorman, C.J.3
  • 58
    • 0025159242 scopus 로고
    • Genetic analysis of an invasion region by use of a Tn3-lac transposon and identification of a second positive regulator gene, invE, for cell invasion of Shigella sonnei: significant homology of invE with ParB of plasmid P1
    • Watanabe H., Arakawa E., Ito K., Kato J., Nakamura A. Genetic analysis of an invasion region by use of a Tn3-lac transposon and identification of a second positive regulator gene, invE, for cell invasion of Shigella sonnei: significant homology of invE with ParB of plasmid P1. J Bacteriol 1990, 172:619-629.
    • (1990) J Bacteriol , vol.172 , pp. 619-629
    • Watanabe, H.1    Arakawa, E.2    Ito, K.3    Kato, J.4    Nakamura, A.5
  • 59
    • 3843113478 scopus 로고    scopus 로고
    • RovA is autoregulated and antagonizes H-NS-mediated silencing of invasin and rovA expression in Yersinia pseudotuberculosis
    • Heroven A.K., Nagel G., Tran H.J., Parr S., Dersch P. RovA is autoregulated and antagonizes H-NS-mediated silencing of invasin and rovA expression in Yersinia pseudotuberculosis. Mol Microbiol 2004, 53:871-888.
    • (2004) Mol Microbiol , vol.53 , pp. 871-888
    • Heroven, A.K.1    Nagel, G.2    Tran, H.J.3    Parr, S.4    Dersch, P.5
  • 61
    • 33745889008 scopus 로고    scopus 로고
    • H-NS represses inv transcription in Yersinia enterocolitica through competition with RovA and interaction with YmoA
    • Ellison D.W., Miller V.L. H-NS represses inv transcription in Yersinia enterocolitica through competition with RovA and interaction with YmoA. J Bacteriol 2006, 188:5101-5112.
    • (2006) J Bacteriol , vol.188 , pp. 5101-5112
    • Ellison, D.W.1    Miller, V.L.2
  • 62
    • 34548674949 scopus 로고    scopus 로고
    • The RovA regulons of Yersinia enterocolitica and Yersinia pestis are distinct: evidence that many RovA-regulated genes were acquired more recently than the core genome
    • Cathelyn J.S., Ellison D.W., Hinchliffe S.J., Wren B.W., Miller V.L. The RovA regulons of Yersinia enterocolitica and Yersinia pestis are distinct: evidence that many RovA-regulated genes were acquired more recently than the core genome. Mol Microbiol 2007, 66:189-205.
    • (2007) Mol Microbiol , vol.66 , pp. 189-205
    • Cathelyn, J.S.1    Ellison, D.W.2    Hinchliffe, S.J.3    Wren, B.W.4    Miller, V.L.5
  • 63
    • 58949087897 scopus 로고    scopus 로고
    • Ler interdomain linker is essential for anti-silencing activity in enteropathogenic Escherichia coli
    • Mellies J.L., Larabee F.J., Zarr M.A., Horback K.L., Lorenzen E., Mavor D. Ler interdomain linker is essential for anti-silencing activity in enteropathogenic Escherichia coli. Microbiology 2008, 154:3624-3638.
    • (2008) Microbiology , vol.154 , pp. 3624-3638
    • Mellies, J.L.1    Larabee, F.J.2    Zarr, M.A.3    Horback, K.L.4    Lorenzen, E.5    Mavor, D.6
  • 64
    • 84901036070 scopus 로고    scopus 로고
    • Locus of enterocyte effacement-encoded regulator (Ler) of pathogenic Escherichia coli competes off histone-like nucleoid-structuring protein (H-NS) through noncooperative DNA binding
    • Winardhi R.S., Gulvady R., Mellies J.L., Yan J. Locus of enterocyte effacement-encoded regulator (Ler) of pathogenic Escherichia coli competes off histone-like nucleoid-structuring protein (H-NS) through noncooperative DNA binding. J Biol Chem 2014, 289:13739-13750.
    • (2014) J Biol Chem , vol.289 , pp. 13739-13750
    • Winardhi, R.S.1    Gulvady, R.2    Mellies, J.L.3    Yan, J.4
  • 66
    • 13444310900 scopus 로고    scopus 로고
    • A truncated H-NS-like protein from enteropathogenic Escherichia coli acts as an H-NS antagonist
    • Williamson H.S., Free A. A truncated H-NS-like protein from enteropathogenic Escherichia coli acts as an H-NS antagonist. Mol Microbiol 2005, 55:808-827.
    • (2005) Mol Microbiol , vol.55 , pp. 808-827
    • Williamson, H.S.1    Free, A.2
  • 67
    • 84904893766 scopus 로고    scopus 로고
    • H-NST induces LEE expression and the formation of attaching and effacing lesions in enterohemorrhagic Escherichia coli
    • Levine J.A., Hansen A.M., Michalski J.M., Hazen T.H., Rasko D.A., Kaper J.B. H-NST induces LEE expression and the formation of attaching and effacing lesions in enterohemorrhagic Escherichia coli. PLOS ONE 2014, 9:e86618.
    • (2014) PLOS ONE , vol.9 , pp. e86618
    • Levine, J.A.1    Hansen, A.M.2    Michalski, J.M.3    Hazen, T.H.4    Rasko, D.A.5    Kaper, J.B.6
  • 68
    • 77950441670 scopus 로고    scopus 로고
    • Identification of the regulatory logic controlling Salmonella pathoadaptation by the SsrA-SsrB two-component system
    • Tomljenovic-Berube A.M., Mulder D.T., Whiteside M.D., Brinkman F.S., Coombes B.K. Identification of the regulatory logic controlling Salmonella pathoadaptation by the SsrA-SsrB two-component system. PLoS Genet 2010, 6:e1000875.
    • (2010) PLoS Genet , vol.6 , pp. e1000875
    • Tomljenovic-Berube, A.M.1    Mulder, D.T.2    Whiteside, M.D.3    Brinkman, F.S.4    Coombes, B.K.5
  • 69
    • 78751479182 scopus 로고    scopus 로고
    • Salmonella enterica response regulator SsrB relieves H-NS silencing by displacing H-NS bound in polymerization mode and directly activates transcription
    • Walthers D., Li Y., Liu Y., Anand G., Yan J., Kenney L.J. Salmonella enterica response regulator SsrB relieves H-NS silencing by displacing H-NS bound in polymerization mode and directly activates transcription. J Biol Chem 2011, 286:1895-1902.
    • (2011) J Biol Chem , vol.286 , pp. 1895-1902
    • Walthers, D.1    Li, Y.2    Liu, Y.3    Anand, G.4    Yan, J.5    Kenney, L.J.6
  • 70
    • 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 R.K., Navarre W.W., Libby S.J., Fang F.C., Kenney L.J. 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 2007, 65:477-493.
    • (2007) Mol Microbiol , vol.65 , pp. 477-493
    • Walthers, D.1    Carroll, R.K.2    Navarre, W.W.3    Libby, S.J.4    Fang, F.C.5    Kenney, L.J.6
  • 71
    • 0034933621 scopus 로고    scopus 로고
    • AraC/XylS family members, HilC and HilD, directly bind and derepress the Salmonella typhimurium hilA promoter
    • Schechter L.M., Lee C.A. AraC/XylS family members, HilC and HilD, directly bind and derepress the Salmonella typhimurium hilA promoter. Mol Microbiol 2001, 40:1289-1299.
    • (2001) Mol Microbiol , vol.40 , pp. 1289-1299
    • Schechter, L.M.1    Lee, C.A.2
  • 72
    • 0037229233 scopus 로고    scopus 로고
    • Transcription of the Salmonella invasion gene activator, hilA, requires HilD activation in the absence of negative regulators
    • Boddicker J.D., Knosp B.M., Jones B.D. Transcription of the Salmonella invasion gene activator, hilA, requires HilD activation in the absence of negative regulators. J Bacteriol 2003, 185:525-533.
    • (2003) J Bacteriol , vol.185 , pp. 525-533
    • Boddicker, J.D.1    Knosp, B.M.2    Jones, B.D.3
  • 73
    • 2342603963 scopus 로고    scopus 로고
    • Contribution of the RpoA C-terminal domain to stimulation of the Salmonella enterica hilA promoter by HilC and HilD
    • Olekhnovich I.N., Kadner R.J. Contribution of the RpoA C-terminal domain to stimulation of the Salmonella enterica hilA promoter by HilC and HilD. J Bacteriol 2004, 186:3249-3253.
    • (2004) J Bacteriol , vol.186 , pp. 3249-3253
    • Olekhnovich, I.N.1    Kadner, R.J.2
  • 74
    • 84907831144 scopus 로고    scopus 로고
    • HilD induces expression of SPI-2 genes by displacing the global negative regulator H-NS from ssrAB
    • Martinez L.C., Banda M.M., Fernandez-Mora M., Santana F.J., Bustamante V.H. HilD induces expression of SPI-2 genes by displacing the global negative regulator H-NS from ssrAB. J Bacteriol 2014, 196:3746-3755.
    • (2014) J Bacteriol , vol.196 , pp. 3746-3755
    • Martinez, L.C.1    Banda, M.M.2    Fernandez-Mora, M.3    Santana, F.J.4    Bustamante, V.H.5
  • 75
    • 84893748866 scopus 로고    scopus 로고
    • Identification of HilD-regulated genes in Salmonella enterica serovar Typhimurium
    • Petrone B.L., Stringer A.M., Wade J.T. Identification of HilD-regulated genes in Salmonella enterica serovar Typhimurium. J Bacteriol 2014, 196:1094-1101.
    • (2014) J Bacteriol , vol.196 , pp. 1094-1101
    • Petrone, B.L.1    Stringer, A.M.2    Wade, J.T.3
  • 76
    • 83655192100 scopus 로고    scopus 로고
    • Integrated stress responses in Salmonella
    • Shen S., Fang F.C. Integrated stress responses in Salmonella. Int J Food Microbiol 2012, 152:75-81.
    • (2012) Int J Food Microbiol , vol.152 , pp. 75-81
    • Shen, S.1    Fang, F.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.