메뉴 건너뛰기




Volumn 55, Issue 3, 2005, Pages 808-827

A truncated H-NS-like protein from enteropathogenic Escherichia coli acts as an H-NS antagonist

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE LIKE NUCLEOID STRUCTURING PROTEIN;

EID: 13444310900     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04421.x     Document Type: Article
Times cited : (60)

References (55)
  • 2
    • 0142012192 scopus 로고    scopus 로고
    • Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: Characterization of the Sfh protein
    • Beloin, C., Deighan, P., Doyle, M., and Dorman, C.J. (2003) Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein. Mol Genet Genomics 270: 66-77.
    • (2003) Mol Genet Genomics , vol.270 , pp. 66-77
    • Beloin, C.1    Deighan, P.2    Doyle, M.3    Dorman, C.J.4
  • 3
    • 0027979044 scopus 로고
    • The H-NS protein is involved in the biogenesis of flagella in Escherichia coli
    • Bertin, P., Terao, E., Lee, E.H., Lejeune, P., Colson, C., Danchin, A., and Collatz, E. (1994) The H-NS protein is involved in the biogenesis of flagella in Escherichia coli. J Bacteriol 176: 5537-5540.
    • (1994) J Bacteriol , vol.176 , pp. 5537-5540
    • Bertin, P.1    Terao, E.2    Lee, E.H.3    Lejeune, P.4    Colson, C.5    Danchin, A.6    Collatz, E.7
  • 4
    • 0032920078 scopus 로고    scopus 로고
    • The structural and functional organization of H-NS-like proteins is evolutionarily conserved in gram-negative bacteria
    • Bertin, P., Benhabiles, N., Krin, E., Laurent-Winter, C., Tendeng, C., Turlin, E., et al. (1999) The structural and functional organization of H-NS-like proteins is evolutionarily conserved in gram-negative bacteria. Mol Microbiol 31: 319-329.
    • (1999) Mol Microbiol , vol.31 , pp. 319-329
    • Bertin, P.1    Benhabiles, N.2    Krin, E.3    Laurent-Winter, C.4    Tendeng, C.5    Turlin, E.6
  • 5
    • 0037336248 scopus 로고    scopus 로고
    • The H-NS dimerization domain defines a new fold contributing to DNA recognition
    • Bloch, V., Yang, Y., Margeat, E., Chavanieu, A., Augé, M.T., Robert, B., et al. (2003) The H-NS dimerization domain defines a new fold contributing to DNA recognition. Nat Struct Biol 10: 212-218.
    • (2003) Nat Struct Biol , vol.10 , pp. 212-218
    • Bloch, V.1    Yang, Y.2    Margeat, E.3    Chavanieu, A.4    Augé, M.T.5    Robert, B.6
  • 6
    • 0035136207 scopus 로고    scopus 로고
    • Transcriptional regulation of type III secretion genes in enteropathogenic Escherichia coli. Ler antagonizes H-NS-dependent repression
    • Bustamante, V.H., Santana, F.J., Calva, E., and Puente, J.L. (2001) Transcriptional regulation of type III secretion genes in enteropathogenic Escherichia coli. Ler antagonizes H-NS-dependent repression. Mol Microbiol 39: 664-678.
    • (2001) Mol Microbiol , vol.39 , pp. 664-678
    • Bustamante, V.H.1    Santana, F.J.2    Calva, E.3    Puente, J.L.4
  • 7
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M.J. (1976) Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 104: 541-555.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 8
    • 0242289355 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae
    • Cerdan, R., Bloch, V., Yang, Y., Bertin, P., Dumas, C., Rimsky, S., et al. (2003) Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae. J Mol Biol 334: 179-185.
    • (2003) J Mol Biol , vol.334 , pp. 179-185
    • Cerdan, R.1    Bloch, V.2    Yang, Y.3    Bertin, P.4    Dumas, C.5    Rimsky, S.6
  • 9
    • 0028340280 scopus 로고
    • Purification of CpG islands using a methylated DNA binding column
    • Cross, S.H., Charlton, J.A., Nan, X., and Bird, A.P. (1994) Purification of CpG islands using a methylated DNA binding column. Nat Genet 6: 236-244.
    • (1994) Nat Genet , vol.6 , pp. 236-244
    • Cross, S.H.1    Charlton, J.A.2    Nan, X.3    Bird, A.P.4
  • 10
    • 0037127209 scopus 로고    scopus 로고
    • Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1
    • Dame, R.T., Wyman, C., Wurm, R., Wagner, R., and Goosen, N. (2002) Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1. J Biol Chem 277: 2146-2150.
    • (2002) J Biol Chem , vol.277 , pp. 2146-2150
    • Dame, R.T.1    Wyman, C.2    Wurm, R.3    Wagner, R.4    Goosen, N.5
  • 11
    • 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., Beloin, C., and Dorman, C.J. (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
  • 12
    • 0027258405 scopus 로고
    • Synthesis of the Escherichia coli K-12 nucleoid-associated DNA-binding protein H-NS is subjected to growth-phase control and autoregulation
    • Dersch, P., Schmidt, K., and Bremer, E. (1993) Synthesis of the Escherichia coli K-12 nucleoid-associated DNA-binding protein H-NS is subjected to growth-phase control and autoregulation. Mol Microbiol 8: 875-889.
    • (1993) Mol Microbiol , vol.8 , pp. 875-889
    • Dersch, P.1    Schmidt, K.2    Bremer, E.3
  • 13
    • 0028036767 scopus 로고
    • The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to a cold environment
    • Dersch, P., Kneip, S., and Bremer, E. (1994) The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to a cold environment. Mol Gen Genet 245: 255-259.
    • (1994) Mol Gen Genet , vol.245 , pp. 255-259
    • Dersch, P.1    Kneip, S.2    Bremer, E.3
  • 14
    • 0032508717 scopus 로고    scopus 로고
    • Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli
    • Donato, G.M., and Kawula, T.H. (1998) Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli. J Biol Chem 273: 24030-24036.
    • (1998) J Biol Chem , vol.273 , pp. 24030-24036
    • Donato, G.M.1    Kawula, T.H.2
  • 15
    • 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. Nature Rev Microbiol 2: 391-400.
    • (2004) Nature Rev Microbiol , vol.2 , pp. 391-400
    • Dorman, C.J.1
  • 16
    • 0033104294 scopus 로고    scopus 로고
    • Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria
    • Dorman, C.J., Hinten, J.C.D., and Free, A. (1999) Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria. Trends Microbiol 7: 124-128.
    • (1999) Trends Microbiol , vol.7 , pp. 124-128
    • Dorman, C.J.1    Hinten, J.C.D.2    Free, A.3
  • 17
    • 0033794502 scopus 로고    scopus 로고
    • The locus of enterocyte effacement (LEE)-encoded regulator controls expression of both LEE- and non-LEE-encoded virulence factors in enteropathogenic and enterohemorrhagic Escherichia coli
    • Elliott, S.J., Sperandio, V., Gíron, J.A., Shin, S., Mellies, J.L., Wainwright, L., et al. (2000) The locus of enterocyte effacement (LEE)-encoded regulator controls expression of both LEE- and non-LEE-encoded virulence factors in enteropathogenic and enterohemorrhagic Escherichia coli. Infect Immun 68: 6115-6126.
    • (2000) Infect Immun , vol.68 , pp. 6115-6126
    • Elliott, S.J.1    Sperandio, V.2    Gíron, J.A.3    Shin, S.4    Mellies, J.L.5    Wainwright, L.6
  • 18
    • 0036928821 scopus 로고    scopus 로고
    • H-NS oligomerization domain structure reveals the mechanism for high order self association of the intact protein
    • Esposito, D., Petrovic, A., Harris, R., Ono, S., Eccleston, J.F., Mbabaali, A., et al. (2002) H-NS oligomerization domain structure reveals the mechanism for high order self association of the intact protein. J Mol Biol 324: 841-850.
    • (2002) J Mol Biol , vol.324 , pp. 841-850
    • Esposito, D.1    Petrovic, A.2    Harris, R.3    Ono, S.4    Eccleston, J.F.5    Mbabaali, A.6
  • 19
    • 0027429067 scopus 로고
    • Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression
    • Falconi, M., Higgins, N.P., Spurio, R., Pon, C.L., and Gualerzi, C.O. (1993) Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression. Mol Microbiol 10: 273-282.
    • (1993) Mol Microbiol , vol.10 , pp. 273-282
    • Falconi, M.1    Higgins, N.P.2    Spurio, R.3    Pon, C.L.4    Gualerzi, C.O.5
  • 20
    • 0028148504 scopus 로고
    • Escherichia coli tyrT gene transcription is sensitive to DNA supercoiling in its native chromosomal context: Effect of DNA topoisomerase IV overexpression on tyrT promoter function
    • Free, A., and Dorman, C.J. (1994) Escherichia coli tyrT gene transcription is sensitive to DNA supercoiling in its native chromosomal context: effect of DNA topoisomerase IV overexpression on tyrT promoter function. Mol Microbiol 14: 151-161.
    • (1994) Mol Microbiol , vol.14 , pp. 151-161
    • Free, A.1    Dorman, C.J.2
  • 21
    • 0031882335 scopus 로고    scopus 로고
    • The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli
    • Free, A., Williams, R.M., and Dorman, C.J. (1998) The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli. J Bacteriol 180: 994-997.
    • (1998) J Bacteriol , vol.180 , pp. 994-997
    • Free, A.1    Williams, R.M.2    Dorman, C.J.3
  • 22
    • 0035167187 scopus 로고    scopus 로고
    • Requirement for the molecular adapter function of StpA at the Escherichia coli bgl promoter depends upon the level of truncated H-NS protein
    • Free, A., Porter, M.E., Deighan, P., and Dorman, C.J. (2001) Requirement for the molecular adapter function of StpA at the Escherichia coli bgl promoter depends upon the level of truncated H-NS protein. Mol Microbiol 42: 903-918.
    • (2001) Mol Microbiol , vol.42 , pp. 903-918
    • Free, A.1    Porter, M.E.2    Deighan, P.3    Dorman, C.J.4
  • 24
    • 0037218281 scopus 로고    scopus 로고
    • Interaction of Ler at the LEE5 (tir) operon of enteropathogenic Escherichia coli
    • Haack, K.R., Robinson, C.L., Miller, K.J., Fowlkes, J.W., and Mellies, J.L. (2003) Interaction of Ler at the LEE5 (tir) operon of enteropathogenic Escherichia coli. Infect Immun 71: 384-392.
    • (2003) Infect Immun , vol.71 , pp. 384-392
    • Haack, K.R.1    Robinson, C.L.2    Miller, K.J.3    Fowlkes, J.W.4    Mellies, J.L.5
  • 25
    • 0033992441 scopus 로고    scopus 로고
    • A set of temperature sensitive-replication/-segregation and temperature resistant plasmid vectors with different copy numbers and in an isogenic background (chloramphenicol, kanamycin, lacZ, repA, par, polA)
    • Hashimoto-Gotoh, T., Yamaguchi, M., Yasojima, K., Tsujimura, A., Wakabayashi, Y., and Watanabe, Y. (2000) A set of temperature sensitive-replication/-segregation and temperature resistant plasmid vectors with different copy numbers and in an isogenic background (chloramphenicol, kanamycin, lacZ, repA, par, polA). Gene 241: 185-191.
    • (2000) Gene , vol.241 , pp. 185-191
    • Hashimoto-Gotoh, T.1    Yamaguchi, M.2    Yasojima, K.3    Tsujimura, A.4    Wakabayashi, Y.5    Watanabe, Y.6
  • 26
    • 0028608807 scopus 로고
    • pOSEX: Vectors for osmotically controlled and finely tuned gene expression in Escherichia coli
    • Herbst, B., Kneip, S., and Bremer, E. (1994) pOSEX: vectors for osmotically controlled and finely tuned gene expression in Escherichia coli. Gene 151: 137-142.
    • (1994) Gene , vol.151 , pp. 137-142
    • Herbst, B.1    Kneip, S.2    Bremer, E.3
  • 27
    • 0023833060 scopus 로고
    • A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli
    • Higgins, C.F., Dorman, C.J., Stirling, D.A., Waddell, L., Booth, I.R., May, G., and Bremer, E. (1988) A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli. Cell 52: 569-584.
    • (1988) Cell , vol.52 , pp. 569-584
    • Higgins, C.F.1    Dorman, C.J.2    Stirling, D.A.3    Waddell, L.4    Booth, I.R.5    May, G.6    Bremer, E.7
  • 28
    • 0029872940 scopus 로고    scopus 로고
    • Construction of mini-F plasmid vectors for plasmid shuffling in Escherichia coli
    • Kato, J., and Ikeda, H. (1996) Construction of mini-F plasmid vectors for plasmid shuffling in Escherichia coli. Gene 170: 141-142.
    • (1996) Gene , vol.170 , pp. 141-142
    • Kato, J.1    Ikeda, H.2
  • 29
    • 0030940269 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli protein secretion is induced in response to conditions similar to those in the gastrointestinal tract
    • Kenny, B., Abe, A., Stein, M., and Finlay, B.B. (1997) Enteropathogenic Escherichia coli protein secretion is induced in response to conditions similar to those in the gastrointestinal tract. Infect Immun 65: 2606-2612.
    • (1997) Infect Immun , vol.65 , pp. 2606-2612
    • Kenny, B.1    Abe, A.2    Stein, M.3    Finlay, B.B.4
  • 30
    • 0033892931 scopus 로고    scopus 로고
    • H-NS-dependent regulation of flagellar synthesis is mediated by a LysR family protein
    • Ko, M., and Park, C. (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
  • 31
    • 0018148992 scopus 로고
    • Escherichia coli strains that cause diarrhoea but do not produce heat-labile or heat-stable enterotoxins and are noninvasive
    • Levine, M.M., Bergquist, E.J., Nalin, D.R., Waterman, D.H., Hornick, R.B., Young, C.R., and Sotman, S. (1978) Escherichia coli strains that cause diarrhoea but do not produce heat-labile or heat-stable enterotoxins and are noninvasive. Lancet 1: 1119-1122.
    • (1978) Lancet , vol.1 , pp. 1119-1122
    • Levine, M.M.1    Bergquist, E.J.2    Nalin, D.R.3    Waterman, D.H.4    Hornick, R.B.5    Young, C.R.6    Sotman, S.7
  • 32
    • 0027450801 scopus 로고
    • Gene 5.5 protein of bacteriophage T7 inhibits the nucleoid protein H-NS of Escherichia coli
    • Liu, Q., and Richardson, C.C. (1993) Gene 5.5 protein of bacteriophage T7 inhibits the nucleoid protein H-NS of Escherichia coli. Proc Natl Acad Sci USA 90: 1761-1765.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1761-1765
    • Liu, Q.1    Richardson, C.C.2
  • 33
    • 0028285269 scopus 로고
    • Interactions of the nucleoid-associated DNA-binding protein H-NS with the regulatory region of the osmotically controlled proU operon of Escherichia coli
    • Lucht, J.M., Dersch, P., Kempf, B., and Bremer, E. (1994) Interactions of the nucleoid-associated DNA-binding protein H-NS with the regulatory region of the osmotically controlled proU operon of Escherichia coli. J Biol Chem 269: 6578-6586.
    • (1994) J Biol Chem , vol.269 , pp. 6578-6586
    • Lucht, J.M.1    Dersch, P.2    Kempf, B.3    Bremer, E.4
  • 34
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., and Stock, J. (1991) Predicting coiled coils from protein sequences. Science 252: 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 35
    • 0024652242 scopus 로고
    • The effect of DnaA protein levels and the rate of initiation at oriC on transcription originating in the ftsQ and ftsA genes: In vivo experiments
    • Masters, M., Paterson, T., Popplewell, A.G., Owen-Hughes, T., Pringle, J.H., and Begg, K.J. (1989) The effect of DnaA protein levels and the rate of initiation at oriC on transcription originating in the ftsQ and ftsA genes: in vivo experiments. Mol Gen Genet 216: 475-483.
    • (1989) Mol Gen Genet , vol.216 , pp. 475-483
    • Masters, M.1    Paterson, T.2    Popplewell, A.G.3    Owen-Hughes, T.4    Pringle, J.H.5    Begg, K.J.6
  • 36
    • 0032998631 scopus 로고    scopus 로고
    • The Per regulon of enteropathogenic Escherichia coli: Identification of a regulatory cascade and a novel transcriptional activator, the locus of enterocyle effacement (LEE)-encoded regulator (Ler)
    • Mellies, J.L., Elliott, S.J., Sperandio, V., Donnenberg, M.S., and Kaper, J.B. (1999) The Per regulon of enteropathogenic Escherichia coli: identification of a regulatory cascade and a novel transcriptional activator, the locus of enterocyle effacement (LEE)-encoded regulator (Ler). Mol Microbiol 33: 296-306.
    • (1999) Mol Microbiol , vol.33 , pp. 296-306
    • Mellies, J.L.1    Elliott, S.J.2    Sperandio, V.3    Donnenberg, M.S.4    Kaper, J.B.5
  • 37
  • 38
    • 0025347043 scopus 로고
    • Pyelonephritogenic Escherichia coli and killing of cultured human renal proximal tubular epithelial cells: Role of hemolysin in some strains
    • Mobley, H.L.T., Green, D.M., Trifillis, A.L., Johnson, D.E., Chippendale, G.R., Lockatell, C.V., et al. (1990) Pyelonephritogenic Escherichia coli and killing of cultured human renal proximal tubular epithelial cells: role of hemolysin in some strains. Infect Immun 58: 1281-1289.
    • (1990) Infect Immun , vol.58 , pp. 1281-1289
    • Mobley, H.L.T.1    Green, D.M.2    Trifillis, A.L.3    Johnson, D.E.4    Chippendale, G.R.5    Lockatell, C.V.6
  • 39
    • 0033797058 scopus 로고    scopus 로고
    • Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS
    • Nieto, J.M., Madrid, C., Prenafeta, A., Miquelay, E., Balsalobre, C., Carrascal, M., et al. (2000) Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS. Mol Gen Genet 263: 349-358.
    • (2000) Mol Gen Genet , vol.263 , pp. 349-358
    • Nieto, J.M.1    Madrid, C.2    Prenafeta, A.3    Miquelay, E.4    Balsalobre, C.5    Carrascal, M.6
  • 40
    • 0036174055 scopus 로고    scopus 로고
    • Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins
    • Nieto, J.M., Madrid, C., Miquelay, E., Parra, J.L., Rodríguez, S., and Juárez, A. (2002) Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins. J Bacteriol 184: 629-635.
    • (2002) J Bacteriol , vol.184 , pp. 629-635
    • Nieto, J.M.1    Madrid, C.2    Miquelay, E.3    Parra, J.L.4    Rodríguez, S.5    Juárez, A.6
  • 41
    • 0032693325 scopus 로고    scopus 로고
    • rpoS function is essential for bgl silencing caused by C-terminally truncated H-NS in Escherichia coli
    • Ohta, T., Ueguchi, C., and Mizuno, T. (1999) rpoS function is essential for bgl silencing caused by C-terminally truncated H-NS in Escherichia coli. J Bacteriol 181: 6278-6283.
    • (1999) J Bacteriol , vol.181 , pp. 6278-6283
    • Ohta, T.1    Ueguchi, C.2    Mizuno, T.3
  • 42
    • 0026754366 scopus 로고
    • The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression
    • Owen-Hughes, T.A., Pavitt, G.D., Santos, D.S., Sidebotham, J.M., Hulton, C.S.J., Hinton, J.C.D., and Higgins, C.F. (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.J.5    Hinton, J.C.D.6    Higgins, C.F.7
  • 43
    • 8544239349 scopus 로고    scopus 로고
    • Direct and indirect transcriptional activation of virulence genes by an AraC-like protein, PerA from enteropathogenic Escherichia coli
    • doi:10.1111/j.1365-2958.2004.04333.x
    • Porter, M.E., Mitchell, P., Roe, A.J., Free, A., Smith, D.G.E., and Gaily, D.L. (2004) Direct and indirect transcriptional activation of virulence genes by an AraC-like protein, PerA from enteropathogenic Escherichia coli. Mol Microbiol doi:10.1111/j.1365-2958.2004.04333.x
    • (2004) Mol Microbiol
    • Porter, M.E.1    Mitchell, P.2    Roe, A.J.3    Free, A.4    Smith, D.G.E.5    Gaily, D.L.6
  • 44
    • 0035830967 scopus 로고    scopus 로고
    • Structural characterization of the N-terminal oligomerization domain of the bacterial chromatin-structuring protein, H-NS
    • Renzoni, D., Esposito, D., Pfuhl, M., Hinton, J.C.D., Higgins, C.F., Driscoll, P.C., and Ladbury, J.E. (2001) Structural characterization of the N-terminal oligomerization domain of the bacterial chromatin-structuring protein, H-NS. J Mol Biol 306: 1127-1137.
    • (2001) J Mol Biol , vol.306 , pp. 1127-1137
    • Renzoni, D.1    Esposito, D.2    Pfuhl, M.3    Hinton, J.C.D.4    Higgins, C.F.5    Driscoll, P.C.6    Ladbury, J.E.7
  • 45
    • 1842453825 scopus 로고    scopus 로고
    • Structure of the histone-like protein H-NS and its role in regulation and genome superstructure
    • Rimsky, S. (2004) Structure of the histone-like protein H-NS and its role in regulation and genome superstructure. Curr Opin Microbiol 7: 109-114.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 109-114
    • Rimsky, S.1
  • 46
    • 0035045615 scopus 로고    scopus 로고
    • Transcriptional regulation of the orf19 gene and the tir-cesT-eae operon of enteropathogenic Escherichia coli
    • Sánchez-SanMartín, C., Bustamante, V.H., Calva, E., and Puente, J.L. (2001) Transcriptional regulation of the orf19 gene and the tir-cesT-eae operon of enteropathogenic Escherichia coli. J Bacteriol 183: 2823-2833.
    • (2001) J Bacteriol , vol.183 , pp. 2823-2833
    • Sánchez-SanMartín, C.1    Bustamante, V.H.2    Calva, E.3    Puente, J.L.4
  • 47
    • 0028900971 scopus 로고
    • Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli
    • Shindo, H., Iwaki, T., Ieda, R., Kurumizaka, H., Ueguchi, C., Mizuno, T., et al. (1995) Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. FEBS Lett 360: 125-131.
    • (1995) FEBS Lett , vol.360 , pp. 125-131
    • Shindo, H.1    Iwaki, T.2    Ieda, R.3    Kurumizaka, H.4    Ueguchi, C.5    Mizuno, T.6
  • 48
    • 0033027096 scopus 로고    scopus 로고
    • Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy
    • Shindo, H., Ohnuki, A., Ginba, H., Katoh, E., Ueguchi, C., Mizuno, T., and Yamazaki, T. (1999) Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy. FEBS Lett 455: 63-69.
    • (1999) FEBS Lett , vol.455 , pp. 63-69
    • Shindo, H.1    Ohnuki, A.2    Ginba, H.3    Katoh, E.4    Ueguchi, C.5    Mizuno, T.6    Yamazaki, T.7
  • 50
    • 0035076860 scopus 로고    scopus 로고
    • The nucleoid-associated protein StpA binds curved DNA, has a greater DNA-binding affinity than H-NS and is present in significant levels in hns mutants
    • Sonnenfield, J.M., Burns, C.M., Higgins, C.F., and Hinton, J.C.D. (2001) The nucleoid-associated protein StpA binds curved DNA, has a greater DNA-binding affinity than H-NS and is present in significant levels in hns mutants. Biochimie 83: 243-249.
    • (2001) Biochimie , vol.83 , pp. 243-249
    • Sonnenfield, J.M.1    Burns, C.M.2    Higgins, C.F.3    Hinton, J.C.D.4
  • 51
    • 0242289416 scopus 로고    scopus 로고
    • H-NS in Gram-negative bacteria: A family of multifaceted proteins
    • Tendeng, C., and Bertin, P.N. (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
  • 52
    • 0030601826 scopus 로고    scopus 로고
    • Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS
    • Ueguchi, C., Suzuki, T., Yoshida, T., Tanaka, K., and Mizuno, T. (1996) Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS. J Mol Biol 263: 149-162.
    • (1996) J Mol Biol , vol.263 , pp. 149-162
    • Ueguchi, C.1    Suzuki, T.2    Yoshida, T.3    Tanaka, K.4    Mizuno, T.5
  • 53
    • 0030663474 scopus 로고    scopus 로고
    • Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS
    • Ueguchi, C., Seto, C., Suzuki, T., and Mizuno, T. (1997) Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS. J Mol Biol 274: 145-151.
    • (1997) J Mol Biol , vol.274 , pp. 145-151
    • Ueguchi, C.1    Seto, C.2    Suzuki, T.3    Mizuno, T.4
  • 54
    • 0037168538 scopus 로고    scopus 로고
    • Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli
    • Welch, R.A., Burland, V., Plunkett, G., 3rd, Redford, P., Roesch, P., Rasko, D., et al. (2002) Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli. Proc Natl Acad Sci USA 99: 17020-17024.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 17020-17024
    • Welch, R.A.1    Burland, V.2    Plunkett III, G.3    Redford, P.4    Roesch, P.5    Rasko, D.6
  • 55
    • 0029785418 scopus 로고    scopus 로고
    • Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using dominant negative derivatives
    • Williams, R.M., Rimsky, S., and Buc, H. (1996) Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using dominant negative derivatives. J Bacteriol 178: 4335-4343.
    • (1996) J Bacteriol , vol.178 , pp. 4335-4343
    • Williams, R.M.1    Rimsky, S.2    Buc, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.