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Volumn 187, Issue 5, 2005, Pages 1845-1848

DNA bridging: A property shared among H-NS-like proteins

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE LIKE NUCLEOID STRUCTURING PROTEIN;

EID: 14244261013     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.5.1845-1848.2005     Document Type: Article
Times cited : (128)

References (31)
  • 2
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • Azam, T. A., and A. Ishihama. 1999. Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274:33105-33113.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 4
    • 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
    • Berlin, 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
    • Berlin, P.1    Hommais, F.2    Krin, E.3    Soutourina, O.4    Tendeng, C.5    Derzelle, S.6    Danchin, A.7
  • 6
    • 0033970889 scopus 로고    scopus 로고
    • Multimeric self-assembly equilibria involving the histone-like protein H-NS. A thermodynamic study
    • Ceschini, S., G. Lupidi, M. Coletta, C. L. Pon, E. Fioretti, and M. Angeletti. 2000. Multimeric self-assembly equilibria involving the histone-like protein H-NS. A thermodynamic study. J. Biol. Chem. 275:729-734.
    • (2000) J. Biol. Chem. , vol.275 , pp. 729-734
    • Ceschini, S.1    Lupidi, G.2    Coletta, M.3    Pon, C.L.4    Fioretti, E.5    Angeletti, M.6
  • 7
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualized by atomic force microscopy
    • Dame, R. T., C. Wyman, and N. Goosen. 2000. H-NS mediated compaction of DNA visualized 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
  • 8
    • 0035083490 scopus 로고    scopus 로고
    • Structural basis for preferential binding of H-NS to curved DNA
    • Dame, R. T., C. Wyraan, and N. Goosen. 2001. Structural basis for preferential binding of H-NS to curved DNA. Biochimie 83:231-234.
    • (2001) Biochimie , vol.83 , pp. 231-234
    • Dame, R.T.1    Wyraan, C.2    Goosen, N.3
  • 9
    • 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., C. Wyman, R. Wurm, R. Wagner, and N. Goosen. 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
  • 10
    • 0344043346 scopus 로고    scopus 로고
    • Protein structure prediction. Implications for the biologist
    • Deleage, G., C. Blanchet, and C. Geourjon. 1997. Protein structure prediction. Implications for the biologist. Biochimie 79:681-686.
    • (1997) Biochimie , vol.79 , pp. 681-686
    • Deleage, G.1    Blanchet, C.2    Geourjon, C.3
  • 11
    • 0036233780 scopus 로고    scopus 로고
    • Advancing the quorum in Pseudomonas aeruginosa: MvaT and the regulation of N-acylhomoserine lactone production and virulence gene expression
    • Diggle, S. P., K. Winzer, A. Lazdunski, P. Williams, and M. Camara. 2002. Advancing the quorum in Pseudomonas aeruginosa: MvaT and the regulation of N-acylhomoserine lactone production and virulence gene expression. J. Bacteriol. 184:2576-2586.
    • (2002) J. Bacteriol. , vol.184 , pp. 2576-2586
    • Diggle, S.P.1    Winzer, K.2    Lazdunski, A.3    Williams, P.4    Camara, M.5
  • 12
    • 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
  • 13
    • 0033104294 scopus 로고    scopus 로고
    • Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria
    • Dorman, C. J., J. C. Hinton, and A. Free. 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    Hinton, J.C.2    Free, A.3
  • 15
    • 0031035206 scopus 로고    scopus 로고
    • The Escherichia coli stpA gene is transiently expressed during growth in rich medium and is induced in minimal medium and by stress conditions
    • Free, A., and C. J. Dorman. 1997. The Escherichia coli stpA gene is transiently expressed during growth in rich medium and is induced in minimal medium and by stress conditions. J. Bacteriol. 179:909-918.
    • (1997) J. Bacteriol. , vol.179 , pp. 909-918
    • Free, A.1    Dorman, C.J.2
  • 16
    • 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., M. E. Porter, P. Deighan, and C. J. Dorman. 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. 42:903-917.
    • (2001) Mol. Microbiol. , vol.42 , pp. 903-917
    • Free, A.1    Porter, M.E.2    Deighan, P.3    Dorman, C.J.4
  • 17
    • 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
  • 18
    • 14244263426 scopus 로고    scopus 로고
    • Major nucleoid proteins in the structure and function of the Escherichia coli chromosome
    • N. P. Higgins (ed.). American Society for Microbiology, Washington, D.C.
    • Johnson, R. C., L. M. Johnson, J. 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. American Society for Microbiology, Washington, D.C.
    • (2005) The Bacterial Chromosome , pp. 65-132
    • Johnson, R.C.1    Johnson, L.M.2    Schmidt, J.3    Gardner, J.F.4
  • 19
    • 0026027810 scopus 로고
    • Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase
    • Munier, H., A. M. Gilles, P. Glaser, E. Krin, A. Danchin, R. Sarfati, and O. Barzu. 1991. Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase. Eur. J. Biochem. 196:469-474.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 469-474
    • Munier, H.1    Gilles, A.M.2    Glaser, P.3    Krin, E.4    Danchin, A.5    Sarfati, R.6    Barzu, O.7
  • 20
    • 1542319979 scopus 로고    scopus 로고
    • Novel physiological modulation of the Pu promoter of TOL plasmid: Negative regulatory role of the TurA protein of Pseudomonas putida in the response to suboptimal growth temperatures
    • Rescalli, E., S. Saini, C. Bartocci, L. Rychlewski, V. De Lorenzo, and G. Bertoni. 2004. Novel physiological modulation of the Pu promoter of TOL plasmid: negative regulatory role of the TurA protein of Pseudomonas putida in the response to suboptimal growth temperatures. J. Biol. Chem. 279:7777-7784.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7777-7784
    • Rescalli, E.1    Saini, S.2    Bartocci, C.3    Rychlewski, L.4    De Lorenzo, V.5    Bertoni, G.6
  • 21
    • 0036332716 scopus 로고    scopus 로고
    • The bacterial regulatory protein H-NS - A versatile modulator of nucleic acid structures
    • Schröder, O., and R. Wagner. 2002. The bacterial regulatory protein H-NS-a versatile modulator of nucleic acid structures. Biol. Chem. 383:945-960.
    • (2002) Biol. Chem. , vol.383 , pp. 945-960
    • Schröder, O.1    Wagner, R.2
  • 22
    • 0027999823 scopus 로고
    • Plasmids bearing hfq and the hns-like gene stpA complement hns mutants in modulating arginine decarboxylase gene expression in Escherichia coli
    • Shi, X., and G. N. Bennett. 1994. Plasmids bearing hfq and the hns-like gene stpA complement hns mutants in modulating arginine decarboxylase gene expression in Escherichia coli. J. Bacteriol. 176:6769-6775.
    • (1994) J. Bacteriol. , vol.176 , pp. 6769-6775
    • Shi, X.1    Bennett, G.N.2
  • 24
    • 0029812469 scopus 로고    scopus 로고
    • Coordinated and differential expression of histone-like proteins in Escherichia coli: Regulation and function of the H-NS analog StpA
    • Sonden, B., and B. E. Uhlin. 1996. Coordinated and differential expression of histone-like proteins in Escherichia coli: regulation and function of the H-NS analog StpA. EMBO J. 15:4970-4980.
    • (1996) EMBO J. , vol.15 , pp. 4970-4980
    • Sonden, B.1    Uhlin, B.E.2
  • 25
    • 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., C. M. Burns, C. F. Higgins, and J. C. Hinton. 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.4
  • 26
    • 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
  • 27
    • 0344118072 scopus 로고    scopus 로고
    • MvaT proteins in Pseudomonas spp.: A novel class of H-NS-like proteins
    • Tendeng, C., O. A. Soutourina, A. Danchin, and P. N. Bertin. 2003. MvaT proteins in Pseudomonas spp.: a novel class of H-NS-like proteins. Microbiology 149:3047-3050.
    • (2003) Microbiology , vol.149 , pp. 3047-3050
    • Tendeng, C.1    Soutourina, O.A.2    Danchin, A.3    Bertin, P.N.4
  • 28
  • 29
    • 0002973783 scopus 로고    scopus 로고
    • Structure of DNA within the bacterial cell: Physics and physiology
    • R. L. Charlebois (ed.). American Society for Microbiology, Washington, D.C.
    • Woldringh, C. L., and T. Odrjk. 1999. Structure of DNA within the bacterial cell: physics and physiology, p. 171-187. In R. L. Charlebois (ed.), Organization of the prokaryotic genome. American Society for Microbiology, Washington, D.C.
    • (1999) Organization of the Prokaryotic Genome , pp. 171-187
    • Woldringh, C.L.1    Odrjk, T.2
  • 30
    • 0027073133 scopus 로고
    • Nucleotide sequence of a newly-identified Escherichia coli gene, stpA, encoding an H-NS-like protein
    • Zhang, A., and M. Belfort. 1992. Nucleotide sequence of a newly-identified Escherichia coli gene, stpA, encoding an H-NS-like protein. Nucleic Acids Res. 20:6735.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6735
    • Zhang, A.1    Belfort, M.2
  • 31
    • 0029913710 scopus 로고    scopus 로고
    • Escherichia coli protein analogs StpA and H-NS: Regulatory loops, similar and disparate effects on nucleic acid dynamics
    • Zhang, A., S. Rimsky, M. E. Reaban, H. Buc, and M. Belfort. 1996. Escherichia coli protein analogs StpA and H-NS: regulatory loops, similar and disparate effects on nucleic acid dynamics. EMBO J. 15:1340-1349.
    • (1996) EMBO J. , vol.15 , pp. 1340-1349
    • Zhang, A.1    Rimsky, S.2    Reaban, M.E.3    Buc, H.4    Belfort, M.5


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