메뉴 건너뛰기




Volumn 190, Issue 21, 2008, Pages 7052-7059

Lsr2 of Mycobacterium represents a novel class of H-NS-like proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA GLUCOSIDASE; GLUCOSIDE; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; PROTEIN LSR 2; UNCLASSIFIED DRUG;

EID: 55749090843     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00733-08     Document Type: Article
Times cited : (94)

References (52)
  • 1
    • 0037238137 scopus 로고    scopus 로고
    • An extended role for the nucleoid structuring protein H-NS in the virulence gene regulatory cascade of Shigella flexneri
    • Beloin, C., and C. J. Dorman. 2003. An extended role for the nucleoid structuring protein H-NS in the virulence gene regulatory cascade of Shigella flexneri. Mol. Microbiol. 47:825-838.
    • (2003) Mol. Microbiol , vol.47 , pp. 825-838
    • Beloin, C.1    Dorman, C.J.2
  • 3
    • 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., F. Hommais, E. Krin, O. Soutourina, C. Tendeng, S. Derzelle, and A. Danchin. 2001. H-NS and H-NS-like proteins in gram-negative bacteria and their multiple role in the regulation of bacterial metabolism. Biochimie 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
  • 6
    • 34247628510 scopus 로고    scopus 로고
    • H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing
    • Bouffartigues, E., M. Buckle, C. Badaut, A. Travers, and S. Rimsky. 2007. H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing. Nat. Struct. Mol. Biol. 14:441-448.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 441-448
    • Bouffartigues, E.1    Buckle, M.2    Badaut, C.3    Travers, A.4    Rimsky, S.5
  • 7
    • 30744468391 scopus 로고    scopus 로고
    • Roles of Lsr2 in colony morphology and biofilm formation of Mycobacterium smegmatis
    • Chen, J. M., G. J. German, D. C. Alexander, H. Ren, T. Tan, and J. Liu. 2006. Roles of Lsr2 in colony morphology and biofilm formation of Mycobacterium smegmatis. J. Bacteriol. 188:633-641.
    • (2006) J. Bacteriol , vol.188 , pp. 633-641
    • Chen, J.M.1    German, G.J.2    Alexander, D.C.3    Ren, H.4    Tan, T.5    Liu, J.6
  • 9
    • 34347333558 scopus 로고    scopus 로고
    • Colangeli, R., D. Helb, C. Vilcheze, M. H. Hazbon, C. G. Lee, H. Safi, B. Sayers, I. Sardone, M. B. Jones, R. D. Fleischmann, S. N. Peterson, W. R. Jacobs, and D. Alland. 2007. Transcriptional regulation of multi-drug tolerance and antibiotic-induced responses by the histone-like protein Lsr2 in M. tuberculosis. PLoS Pathog. 3:e87.
    • Colangeli, R., D. Helb, C. Vilcheze, M. H. Hazbon, C. G. Lee, H. Safi, B. Sayers, I. Sardone, M. B. Jones, R. D. Fleischmann, S. N. Peterson, W. R. Jacobs, and D. Alland. 2007. Transcriptional regulation of multi-drug tolerance and antibiotic-induced responses by the histone-like protein Lsr2 in M. tuberculosis. PLoS Pathog. 3:e87.
  • 10
    • 18444369954 scopus 로고    scopus 로고
    • The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin
    • Dame, R. T. 2005. The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin. Mol. Microbiol. 56:858-870.
    • (2005) Mol. Microbiol , vol.56 , pp. 858-870
    • Dame, R.T.1
  • 12
    • 33751098486 scopus 로고    scopus 로고
    • Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation
    • Dame, R. T., M. C. Noom, and G. J. Wuite. 2006. Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation. Nature 444:387-390.
    • (2006) Nature , vol.444 , pp. 387-390
    • Dame, R.T.1    Noom, M.C.2    Wuite, G.J.3
  • 13
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame, R. T., C. Wyman, and N. Goosen. 2000. H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res. 28:3504-3510.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 14
    • 0019348090 scopus 로고
    • Cryptic operon for beta-glucoside metabolism in Escherichia coli K12: Genetic evidence for a regulatory protein
    • Defez, R., and M. De Felice. 1981. Cryptic operon for beta-glucoside metabolism in Escherichia coli K12: genetic evidence for a regulatory protein. Genetics 97:11-25.
    • (1981) Genetics , vol.97 , pp. 11-25
    • Defez, R.1    De Felice, M.2
  • 15
    • 0038120866 scopus 로고    scopus 로고
    • Three-way interactions among the Sfh, StpA and H-NS nucleoid-structuring proteins of Shigella flexneri 2a strain 2457T
    • Deighan, P., C. Beloin, and C. J. Dorman. 2003. Three-way interactions among the Sfh, StpA and H-NS nucleoid-structuring proteins of Shigella flexneri 2a strain 2457T. Mol. Microbiol. 48:1401-1416.
    • (2003) Mol. Microbiol , vol.48 , pp. 1401-1416
    • Deighan, P.1    Beloin, C.2    Dorman, C.J.3
  • 16
    • 1942532920 scopus 로고    scopus 로고
    • The histone-like nucleoid structuring protein H-NS represses the Escherichia coli bgl operon downstream of the promoter
    • Dole, S., V. Nagarajavel, and K. Schnetz. 2004. The histone-like nucleoid structuring protein H-NS represses the Escherichia coli bgl operon downstream of the promoter. Mol. Microbiol. 52:589-600.
    • (2004) Mol. Microbiol , vol.52 , pp. 589-600
    • Dole, S.1    Nagarajavel, V.2    Schnetz, K.3
  • 17
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: A universal regulator for a dynamic genome
    • Dorman, C. J. 2004. H-NS: a universal regulator for a dynamic genome. Nat. Rev. Microbiol. 2:391-400.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 391-400
    • Dorman, C.J.1
  • 18
    • 33745889008 scopus 로고    scopus 로고
    • H-NS represses inv transcription in Yersinia enterocolitica through competition with RovA and interaction with YmoA
    • Ellison, D. W., and V. L. Miller. 2006. H-NS represses inv transcription in Yersinia enterocolitica through competition with RovA and interaction with YmoA. J. Bacteriol. 188:5101-5112.
    • (2006) J. Bacteriol , vol.188 , pp. 5101-5112
    • Ellison, D.W.1    Miller, V.L.2
  • 20
    • 0032401769 scopus 로고    scopus 로고
    • Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS
    • Falconi, M., B. Colonna, G. Prosseda, G. Micheli, and C. O. Gualerzi. 1998. Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS. EMBO J. 17:7033-7043.
    • (1998) EMBO J , vol.17 , pp. 7033-7043
    • Falconi, M.1    Colonna, B.2    Prosseda, G.3    Micheli, G.4    Gualerzi, C.O.5
  • 21
    • 0030065921 scopus 로고    scopus 로고
    • Hns mutant unveils the presence of a latent haemolytic activity in Escherichia coli K-12
    • Gomez-Gomez, J. M., J. Blazquez, F. Baquero, and J. L. Martinez. 1996. Hns mutant unveils the presence of a latent haemolytic activity in Escherichia coli K-12. Mol. Microbiol. 19:909-910.
    • (1996) Mol. Microbiol , vol.19 , pp. 909-910
    • Gomez-Gomez, J.M.1    Blazquez, J.2    Baquero, F.3    Martinez, J.L.4
  • 22
    • 0030916257 scopus 로고    scopus 로고
    • Characterization of BpH3, an H-NS-like protein in Bordetella pertussis
    • Goyard, S., and P. Bertin. 1997. Characterization of BpH3, an H-NS-like protein in Bordetella pertussis. Mol. Microbiol. 24:815-823.
    • (1997) Mol. Microbiol , vol.24 , pp. 815-823
    • Goyard, S.1    Bertin, P.2
  • 23
    • 33750000118 scopus 로고    scopus 로고
    • Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome
    • Grainger, D. C., D. Hurd, M. D. Goldberg, and S. J. Busby. 2006. Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome. Nucleic Acids Res. 34:4642-4652.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4642-4652
    • Grainger, D.C.1    Hurd, D.2    Goldberg, M.D.3    Busby, S.J.4
  • 25
    • 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., G. Nagel, H. J. Tran, S. Parr, and P. Dersch. 2004. RovA is autoregulated and antagonizes H-NS-mediated silencing of invasin and rovA expression in Yersinia pseudotuberculosis. Mol. Microbiol. 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
  • 26
    • 0026661849 scopus 로고
    • Expression and mutational analysis of the nucleoid-associated protein H-NS of Salmonella typhimurium
    • Hinton, J. C., D. S. Santos, A. Seirafi, C. S. Hulton, G. D. Pavitt, and C. F. Higgins. 1992. Expression and mutational analysis of the nucleoid-associated protein H-NS of Salmonella typhimurium. Mol. Microbiol. 6:2327-2337.
    • (1992) Mol. Microbiol , vol.6 , pp. 2327-2337
    • Hinton, J.C.1    Santos, D.S.2    Seirafi, A.3    Hulton, C.S.4    Pavitt, G.D.5    Higgins, C.F.6
  • 28
    • 0028805887 scopus 로고
    • Color selection with a hygromycin-resistance-based Escherichia coli-mycobacterial shuttle vector
    • Howard, N. S., J. E. Gomez, C. Ko, and W. R. Bishai. 1995. Color selection with a hygromycin-resistance-based Escherichia coli-mycobacterial shuttle vector. Gene 166:181-182.
    • (1995) Gene , vol.166 , pp. 181-182
    • Howard, N.S.1    Gomez, J.E.2    Ko, C.3    Bishai, W.R.4
  • 29
    • 14244263426 scopus 로고    scopus 로고
    • Major nucleoid proteins in the structure and function of the Escherichia coli chromosome
    • N. P. Higgins ed, ASM Press, Washington, DC
    • Johnson, R. C., M. J. Johnson, J. W. Schmidt, and J. F. Gardner. 2005. Major nucleoid proteins in the structure and function of the Escherichia coli chromosome, p. 65-132. In N. P. Higgins (ed.), The bacterial chromosome. ASM Press, Washington, DC.
    • (2005) The bacterial chromosome , pp. 65-132
    • Johnson, R.C.1    Johnson, M.J.2    Schmidt, J.W.3    Gardner, J.F.4
  • 30
    • 0033900163 scopus 로고    scopus 로고
    • Analysis of the beta-glucoside utilization (bgl) genes of Shigella sonnei: Evolutionary implications for their maintenance in a cryptic state
    • Kharat, A. S., and S. Mahadevan. 2000. Analysis of the beta-glucoside utilization (bgl) genes of Shigella sonnei: evolutionary implications for their maintenance in a cryptic state. Microbiology 146:2039-2049.
    • (2000) Microbiology , vol.146 , pp. 2039-2049
    • Kharat, A.S.1    Mahadevan, S.2
  • 31
    • 0033892931 scopus 로고    scopus 로고
    • H-NS-dependent regulation of flagellar synthesis is mediated by a LysR family protein
    • Ko, M., and C. Park. 2000. H-NS-dependent regulation of flagellar synthesis is mediated by a LysR family protein. J. Bacteriol. 182:4670-4672.
    • (2000) J. Bacteriol , vol.182 , pp. 4670-4672
    • Ko, M.1    Park, C.2
  • 32
    • 49349101279 scopus 로고    scopus 로고
    • Spontaneous transposition of IS1096 or ISMsm3 leads to glycopeptidolipid overproduction and affects surface properties in Mycobacterium smegmatis
    • Kocincova, D., A. K. Singh, J. L. Beretti, H. Ren, D. Euphrasie, J. Liu, M. Daffe, G. Etienne, and J. M. Reyrat. 2008. Spontaneous transposition of IS1096 or ISMsm3 leads to glycopeptidolipid overproduction and affects surface properties in Mycobacterium smegmatis. Tuberculosis (Edinburgh) 88:390-398.
    • (2008) Tuberculosis (Edinburgh) , vol.88 , pp. 390-398
    • Kocincova, D.1    Singh, A.K.2    Beretti, J.L.3    Ren, H.4    Euphrasie, D.5    Liu, J.6    Daffe, M.7    Etienne, G.8    Reyrat, J.M.9
  • 34
    • 0029589218 scopus 로고
    • SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli
    • Ludwig, A., C. Tengel, S. Bauer, A. Bubert, R. Benz, H. J. Mollenkopf, and W. Goebel. 1995. SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli. Mol. Gen. Genet. 249:474-486.
    • (1995) Mol. Gen. Genet , vol.249 , pp. 474-486
    • Ludwig, A.1    Tengel, C.2    Bauer, S.3    Bubert, A.4    Benz, R.5    Mollenkopf, H.J.6    Goebel, W.7
  • 35
    • 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., M. McClelland, S. J. Libby, and F. C. Fang. 2007. Silencing of xenogeneic DNA by H-NS-facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA. Genes Dev. 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
  • 36
    • 33746008173 scopus 로고    scopus 로고
    • Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella
    • Navarre, W. W., S. Porwollik, Y. Wang, M. McClelland, H. Rosen, S. J. Libby, and F. C. Fang. 2006. Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella. Science 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
  • 37
    • 35548978064 scopus 로고    scopus 로고
    • H-NS promotes looped domain formation in the bacterial chromosome
    • Noom, M. C., W. W. Navarre, T. Oshima, G. J. Wuite, and R. T. Dame. 2007. H-NS promotes looped domain formation in the bacterial chromosome. Curr. Biol. 17:R913-R914.
    • (2007) Curr. Biol , vol.17
    • Noom, M.C.1    Navarre, W.W.2    Oshima, T.3    Wuite, G.J.4    Dame, R.T.5
  • 38
    • 0033941006 scopus 로고    scopus 로고
    • Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade
    • Nye, M. B., J. D. Pfau, K. Skorupski, and R. K. Taylor. 2000. Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade. J. Bacteriol. 182:4295-4303.
    • (2000) J. Bacteriol , vol.182 , pp. 4295-4303
    • Nye, M.B.1    Pfau, J.D.2    Skorupski, K.3    Taylor, R.K.4
  • 39
    • 33750898424 scopus 로고    scopus 로고
    • Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase
    • Oshima, T., S. Ishikawa, K. Kurokawa, H. Aiba, and N. Ogasawara. 2006. Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase. DNA Res. 13:141-153.
    • (2006) DNA Res , vol.13 , pp. 141-153
    • Oshima, T.1    Ishikawa, S.2    Kurokawa, K.3    Aiba, H.4    Ogasawara, N.5
  • 40
    • 0026754366 scopus 로고
    • The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression
    • Owen-Hughes, T. A., G. D. Pavitt, D. S. Santos, J. M. Sidebotham, C. S. Hulton, J. C. Hinton, and C. F. Higgins. 1992. The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression. Cell 71:255-265.
    • (1992) Cell , vol.71 , pp. 255-265
    • Owen-Hughes, T.A.1    Pavitt, G.D.2    Santos, D.S.3    Sidebotham, J.M.4    Hulton, C.S.5    Hinton, J.C.6    Higgins, C.F.7
  • 41
    • 0028095884 scopus 로고
    • A role for H-NS in the thermo-osmotic regulation of virulence gene expression in Shigella flexneri
    • Porter, M. E., and C. J. Dorman. 1994. A role for H-NS in the thermo-osmotic regulation of virulence gene expression in Shigella flexneri. J. Bacteriol. 176:4187-4191.
    • (1994) J. Bacteriol , vol.176 , pp. 4187-4191
    • Porter, M.E.1    Dorman, C.J.2
  • 43
    • 0036260547 scopus 로고    scopus 로고
    • Regulation of bacterial motility in response to low pH in Escherichia coli: The role of H-NS protein
    • Soutourina, O. A., E. Krin, C. Laurent-Winter, F. Hommais, A. Danchin, and P. N. Bertin. 2002. Regulation of bacterial motility in response to low pH in Escherichia coli: the role of H-NS protein. Microbiology 148:1543-1551.
    • (2002) Microbiology , vol.148 , pp. 1543-1551
    • Soutourina, O.A.1    Krin, E.2    Laurent-Winter, C.3    Hommais, F.4    Danchin, A.5    Bertin, P.N.6
  • 45
    • 0034102966 scopus 로고    scopus 로고
    • Isolation and characterization of vicH, encoding a new pleiotropic regulator in Vibrio cholerae
    • Tendeng, C., C. Badaut, E. Krin, P. Gounon, S. Ngo, A. Danchin, S. Rimsky, and P. Bertin. 2000. Isolation and characterization of vicH, encoding a new pleiotropic regulator in Vibrio cholerae. J. Bacteriol. 182:2026-2032.
    • (2000) J. Bacteriol , vol.182 , pp. 2026-2032
    • Tendeng, C.1    Badaut, C.2    Krin, E.3    Gounon, P.4    Ngo, S.5    Danchin, A.6    Rimsky, S.7    Bertin, P.8
  • 46
    • 0242289416 scopus 로고    scopus 로고
    • H-NS in gram-negative bacteria: A family of multifaceted proteins
    • Tendeng, C., and P. N. Bertin. 2003. H-NS in gram-negative bacteria: a family of multifaceted proteins. Trends Microbiol. 11:511-518.
    • (2003) Trends Microbiol , vol.11 , pp. 511-518
    • Tendeng, C.1    Bertin, P.N.2
  • 47
    • 0038143249 scopus 로고    scopus 로고
    • A novel H-NS-like protein from an Antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability
    • Tendeng, C., E. Krin, O. A. Soutourina, A. Marin, A. Danchin, and P. N. Bertin. 2003. A novel H-NS-like protein from an Antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability. J. Biol. Chem. 278:18754-18760.
    • (2003) J. Biol. Chem , vol.278 , pp. 18754-18760
    • Tendeng, C.1    Krin, E.2    Soutourina, O.A.3    Marin, A.4    Danchin, A.5    Bertin, P.N.6
  • 48
    • 55749096526 scopus 로고    scopus 로고
    • Thomason, L. C., N. Costantino, and D. L. Court. 2007. E. coli genome manipulation by P1 transduction. Curr. Protoc. Mol. Biol. 79:1.17.1-1.17.8.
    • Thomason, L. C., N. Costantino, and D. L. Court. 2007. E. coli genome manipulation by P1 transduction. Curr. Protoc. Mol. Biol. 79:1.17.1-1.17.8.
  • 49
    • 0029764208 scopus 로고    scopus 로고
    • Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein
    • Timchenko, T., A. Bailone, and R. Devoret. 1996. Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein. EMBO J. 15:3986-3992.
    • (1996) EMBO J , vol.15 , pp. 3986-3992
    • Timchenko, T.1    Bailone, A.2    Devoret, R.3
  • 51
    • 0032918010 scopus 로고    scopus 로고
    • Identification of Fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry
    • Wong, D. K., B.-Y. Lee, M. A. Horwitz, and B. W. Gibson. 1999. Identification of Fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Infect. Immun. 67:327-336.
    • (1999) Infect. Immun , vol.67 , pp. 327-336
    • Wong, D.K.1    Lee, B.-Y.2    Horwitz, M.A.3    Gibson, B.W.4
  • 52
    • 1542286940 scopus 로고    scopus 로고
    • Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA
    • Wyborn, N. R., M. R. Stapleton, V. A. Norte, R. E. Roberts, J. Grafton, and J. Green. 2004. Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA. J. Bacteriol. 186:1620-1628.
    • (2004) J. Bacteriol , vol.186 , pp. 1620-1628
    • Wyborn, N.R.1    Stapleton, M.R.2    Norte, V.A.3    Roberts, R.E.4    Grafton, J.5    Green, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.