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Lammi M., Paci M., Pon C.L., Losso M.A., Miano A., Pawlik R.T., Gianfranceschi G.L., Gualerzi C.O. Proteins from the prokaryotic nucleoid: biochemical and 1H NMR studies on three bacterial histone-like proteins. Adv Exp Med Biol. 179:1984;467-477.
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This is the first review presenting a phyletic distribution of H-NS related proteins. An initial attempt at a phylogenetic type classification showing interesting differences and similarities for the members of the H-NS family is presented.
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Tendeng C., Bertin P.N. H-NS in Gram-negative bacteria: a family of multifaceted proteins. Trends Microbiol. 11:2003;511-518 This is the first review presenting a phyletic distribution of H-NS related proteins. An initial attempt at a phylogenetic type classification showing interesting differences and similarities for the members of the H-NS family is presented.
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Hommais F., Krin E., Laurent-Winter C., Soutourina O., Malpertuy A., Le Caer J.P., Danchin A., Bertin P. Large-scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid-associated protein, H-NS. Mol Microbiol. 40:2001;20-36.
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A molecular mechanism for the repression of transcription by the H-NS protein
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Rimsky S., Zuber F., Buckle M., Buc H. A molecular mechanism for the repression of transcription by the H-NS protein. Mol Microbiol. 42:2001;1311-1323.
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Smyth C.P., Lundback T., Renzoni D., Siligardi G., Beavil R., Layton M., Sidebotham J.M., Hinton J.C., Driscoll P.C., Higgins C.F., Ladbury J.E. Oligomerization of the chromatin-structuring protein H-NS. Mol Microbiol. 36:2000;962-972.
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Schroder O., Tippner D., Wagner R. Toward the three-dimensional structure of the Escherichia coli DNA-binding protein H-NS: a CD and fluorescence study. Biochem Biophys Res Commun. 282:2001;219-227.
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The H-NS dimerization domain defines a new fold contributing to DNA recognition
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This manuscript describes a model for the three-dimensional structure of the amino-terminal part of the Escherichia coli H-NS. The authors also showed that two conserved amino acids from this domain of the protein are important for specific DNA binding.
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Bloch V., Yang Y., Margeat E., Chavanieu A., Auge M.T., Robert B., Arold S., Rimsky S., Kochoyan M. The H-NS dimerization domain defines a new fold contributing to DNA recognition. Nat Struct Biol. 10:2003;212-218 This manuscript describes a model for the three-dimensional structure of the amino-terminal part of the Escherichia coli H-NS. The authors also showed that two conserved amino acids from this domain of the protein are important for specific DNA binding.
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Bloch, V.1
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0035830967
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Structural characterization of the N-terminal oligomerization domain of the bacterial chromatin-structuring protein, H-NS
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Renzoni D., Esposito D., Pfuhl M., Hinton J.C., Higgins C.F., Driscoll P.C., Ladbury J.E. Structural characterization of the N-terminal oligomerization domain of the bacterial chromatin-structuring protein, H-NS. J Mol Biol. 306:2001;1127-1137.
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H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein
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This is the first description of a model for the three-dimensional structure of the amino terminal part of Salmonella typhimurium H-NS. This paper also proposed a scheme of a head to tail association of the H-NS proteins on the DNA.
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Esposito D., Petrovic A., Harris R., Ono S., Eccleston J.F., Mbabaali A., Haq I., Higgins C.F., Hinton J.C., Driscoll P.C., Ladbury J.E. H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein. J Mol Biol. 324:2002;841-850 This is the first description of a model for the three-dimensional structure of the amino terminal part of Salmonella typhimurium H-NS. This paper also proposed a scheme of a head to tail association of the H-NS proteins on the DNA.
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Esposito, D.1
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Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae
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The third three-dimensional model of a H-NS-like protein presented here confirmed the presence of an antiparallel coiled-coil. It shows that VicH and H-NS of E. coli have a very similar fold in their amino terminus.
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Cerdan R., Bloch V., Yang Y., Bertin P., Dumas C., Rimsky S., Kochoyan M., Arold S.T. Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae. J Mol Biol. 334:2003;179-185 The third three-dimensional model of a H-NS-like protein presented here confirmed the presence of an antiparallel coiled-coil. It shows that VicH and H-NS of E. coli have a very similar fold in their amino terminus.
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Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS
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Ueguchi C., Seto C., Suzuki T., Mizuno T. Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS. J Mol Biol. 274:1997;145-151.
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Nye M.B., Taylor R.K. Vibrio cholerae H-NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H-NS family members. Mol Microbiol. 50:2003;427-444.
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Dorman C.J., Hinton J.C., Free A. Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria. Trends Microbiol. 7:1999;124-128.
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Heteromeric interactions among nucleoid-associated bacterial proteins: Localization of StpA-stabilizing regions in H-NS of Escherichia coli
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Johansson J., Eriksson S., Sonden B., Wai S.N., Uhlin B.E. Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli. J Bacteriol. 183:2001;2343-2347.
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Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: Characterization of the Sfh protein
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Beloin C., Deighan P., Doyle M., Dorman C.J. Shigella flexneri 2a strain 2457T expresses three members of the H-NS-like protein family: characterization of the Sfh protein. Mol Genet Genomics. 270:2003;66-77.
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Three-way interactions among the Sfh, StpA and H-NS nucleoid-structuring proteins of Shigella flexneri 2a strain 2457T
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Shigella flexeneri 2a strain 2457T expresses three members of the H-NS family: SpH, StpA and H-NS. This is the first description of a three-way interaction among H-NS-like proteins in the same bacteria. It is shown that the regulation of sph is phase dependent. These three proteins negatively regulate their own genes and cross repress transcription of each other's promoter. Using a two-hybrid system it was shown that they can form heteromers and homomers.
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Deighan P., Beloin C., Dorman C.J. Three-way interactions among the Sfh, StpA and H-NS nucleoid-structuring proteins of Shigella flexneri 2a strain 2457T. Mol Microbiol. 48:2003;1401-1416 Shigella flexeneri 2a strain 2457T expresses three members of the H-NS family: SpH, StpA and H-NS. This is the first description of a three-way interaction among H-NS-like proteins in the same bacteria. It is shown that the regulation of sph is phase dependent. These three proteins negatively regulate their own genes and cross repress transcription of each other's promoter. Using a two-hybrid system it was shown that they can form heteromers and homomers.
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A novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability
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Tendeng C., Krin E., Soutourina O.A., Marin A., Danchin A., Bertin P.N. 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. 278:2003;18754-18760.
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Badaut C., Williams R., Arluison V., Bouffartigues E., Robert B., Buc H., Rimsky S. The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA. J Biol Chem. 277:2002;41657- 41666.
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Dame R.T., Wyman C., Goosen N. H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res. 28:2000;3504-3510.
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Madrid C., Nieto J.M., Paytubi S., Falconi M., Gualerzi C.O., Juarez A. Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin. J Bacteriol. 184:2002;5058-5066.
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The virF promoter in Shigella: More than just a curved DNA stretch
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The virF promoter possesses two H-NS binding regions separated by an intrinsically curved DNA region. The authors described how the DNA geometry through the modulation of the bend, is implied in thermoregulation of this promoter, thus underlying the possible direct role of the DNA as a thermosensor through the modulation of FIS and H-NS binding.
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Prosseda G., Falconi M., Giangrossi M., Gualerzi C.O., Micheli G., Colonna B. The virF promoter in Shigella: more than just a curved DNA stretch. Mol Microbiol. 51:2003;523-537 The virF promoter possesses two H-NS binding regions separated by an intrinsically curved DNA region. The authors described how the DNA geometry through the modulation of the bend, is implied in thermoregulation of this promoter, thus underlying the possible direct role of the DNA as a thermosensor through the modulation of FIS and H-NS binding.
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Mol Microbiol
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Prosseda, G.1
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