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Volumn 24, Issue 16, 2005, Pages 2896-2905

Nature and mechanism of the in vivo oligomerization of nucleoid protein H-NS

Author keywords

Protein dimerization and tetramerization; Transcriptional repression; Two hybrid system

Indexed keywords

HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; MONOMER; TETRAMER;

EID: 28844463650     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600754     Document Type: Article
Times cited : (48)

References (40)
  • 1
    • 0030972952 scopus 로고    scopus 로고
    • H-NS, a modulator of environmentally regulated gene expression
    • Atlung T, Ingmer H (1997) H-NS, a modulator of environmentally regulated gene expression. Mol Microbiol 24: 7-17
    • (1997) Mol Microbiol , vol.24 , pp. 7-17
    • Atlung, T.1    Ingmer, H.2
  • 2
    • 0026552342 scopus 로고
    • KorB protein of promiscuous plasmid RP4 recognizes inverted sequence repetitions in regions essential for conjugative plasmid transfer
    • Balzer D, Ziegelin G, Pansegrau W, Kruft V, Lanka E (1992) KorB protein of promiscuous plasmid RP4 recognizes inverted sequence repetitions in regions essential for conjugative plasmid transfer. Nucleic Acids Res 20: 1851-1858
    • (1992) Nucleic Acids Res , vol.20 , pp. 1851-1858
    • Balzer, D.1    Ziegelin, G.2    Pansegrau, W.3    Kruft, V.4    Lanka, E.5
  • 3
    • 0027874441 scopus 로고
    • Isolation of lambda repressor mutants with defects in cooperative operator binding
    • Beckett D, Burz DS, Ackers GK, Sauer RT (1993) Isolation of lambda repressor mutants with defects in cooperative operator binding. Biochemistry 32: 9073-9079
    • (1993) Biochemistry , vol.32 , pp. 9073-9079
    • Beckett, D.1    Burz, D.S.2    Ackers, G.K.3    Sauer, R.T.4
  • 6
    • 0033970889 scopus 로고    scopus 로고
    • Multimeric self-assembly equilibria involving the histone-like protein H-NS. A thermodynamic study
    • Ceschini S, Lupidi G, Coletta M, Pon CL, Fioretti E, Angeletti M (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
    • 0242668713 scopus 로고    scopus 로고
    • DNA-stimulated assembly of oligomeric bacteriophage 434 repressor: Evidence for cooperative binding by recruitment
    • Ciubotaru M, Koudelka GB (2003) DNA-stimulated assembly of oligomeric bacteriophage 434 repressor: evidence for cooperative binding by recruitment. Biochemistry 42: 4253-4264
    • (2003) Biochemistry , vol.42 , pp. 4253-4264
    • Ciubotaru, M.1    Koudelka, G.B.2
  • 8
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame RT, Wyman C, Goosen N (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
  • 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 RT, Wyman C, Wurm R, Wagner R, 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
  • 10
    • 0037040226 scopus 로고    scopus 로고
    • An Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4
    • Delbruck H, Ziegelin G, Lanka E, Heinemann U (2002) An Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4. J Biol Chem 277: 4191-4198
    • (2002) J Biol Chem , vol.277 , pp. 4191-4198
    • Delbruck, H.1    Ziegelin, G.2    Lanka, E.3    Heinemann, U.4
  • 11
    • 0034969907 scopus 로고    scopus 로고
    • A two-hybrid system based on chimeric recognition for studying protein homo-heterodimerization in Escherichia coli
    • Di Lallo G, Castagnoli L, Ghelardini P, Paolozzi L (2001) A two-hybrid system based on chimeric recognition for studying protein homo- heterodimerization in Escherichia coli. Microbiology 147: 1651-1656
    • (2001) Microbiology , vol.147 , pp. 1651-1656
    • Di Lallo, G.1    Castagnoli, L.2    Ghelardini, P.3    Paolozzi, L.4
  • 12
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: A universal regulator for a dynamic genome
    • Dorman CJ (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
  • 14
    • 0029880342 scopus 로고    scopus 로고
    • Antagonistic involvement of FIS and H-NS proteins in the transcriptional control of hns expression
    • Falconi M, Brandi A, La Teana A, Gualerzi CO, Pon CL (1996) Antagonistic involvement of FIS and H-NS proteins in the transcriptional control of hns expression. Mol Microbiol 19: 965-975
    • (1996) Mol Microbiol , vol.19 , pp. 965-975
    • Falconi, M.1    Brandi, A.2    La Teana, A.3    Gualerzi, C.O.4    Pon, C.L.5
  • 15
    • 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, Colonna B, Prosseda G, Micheli G, Gualerzi CO (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
  • 16
    • 0024004997 scopus 로고
    • Proteins from the prokaryotic nucleoid: Primary and quaternary structure of the 15-kD Escherichia coli DNA-binding protein H-NS
    • Falconi M, Gualtieri MT, La Teana A, Losso MA, Pon CL (1988) Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA-binding protein H-NS. Mol Microbiol 2: 323-329
    • (1988) Mol Microbiol , vol.2 , pp. 323-329
    • Falconi, M.1    Gualtieri, M.T.2    La Teana, A.3    Losso, M.A.4    Pon, C.L.5
  • 17
    • 0012000308 scopus 로고
    • Proteins from the prokaryotic nucleoid. Structural and functional characterization of Eschenchia coli DNA-binding proteins NS (HU) and H-NS
    • Gualerzi CO, Pon CL (eds) Heidelberg: Springer-Verlag
    • Gualerzi CO, Lammi M, Losso MA, Friedrich K, Pawlik RT, Canonaco MA, Gianfranceschi G, Pingoud A, Pon CL (1986) Proteins from the prokaryotic nucleoid. Structural and functional characterization of Eschenchia coli DNA-binding proteins NS (HU) and H-NS. in Bacterial Chromatin, Gualerzi CO, Pon CL (eds) pp 101-134. Heidelberg: Springer-Verlag
    • (1986) Bacterial Chromatin , pp. 101-134
    • Gualerzi, C.O.1    Lammi, M.2    Losso, M.A.3    Friedrich, K.4    Pawlik, R.T.5    Canonaco, M.A.6    Gianfranceschi, G.7    Pingoud, A.8    Pon, C.L.9
  • 19
    • 0030985973 scopus 로고    scopus 로고
    • DNA binding is not sufficient for H-NS-mediated repression of proU expression
    • Jordi BJ, Fielder AE, Burns CM (1997) DNA binding is not sufficient for H-NS-mediated repression of proU expression. J Biol Chem 272: 12083-12090
    • (1997) J Biol Chem , vol.272 , pp. 12083-12090
    • Jordi, B.J.1    Fielder, A.E.2    Burns, C.M.3
  • 20
    • 3042642002 scopus 로고    scopus 로고
    • Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB
    • Khare D, Ziegelin G, Lanka E, Heinemann U (2004) Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. Nat Struct Mol Biol 11: 656-663
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 656-663
    • Khare, D.1    Ziegelin, G.2    Lanka, E.3    Heinemann, U.4
  • 22
    • 0007715651 scopus 로고
    • Structure of chloramphenicol acetyltransferase at 1.75-Å resolution
    • Leslie AG, Moody PC, Shaw WV (1988) Structure of chloramphenicol acetyltransferase at 1.75-Å resolution. Proc Natl Acad Sci USA 85: 4133-4137
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4133-4137
    • Leslie, A.G.1    Moody, P.C.2    Shaw, W.V.3
  • 23
    • 0023051656 scopus 로고
    • Proteins from the prokaryotic nucleoid. A protein-protein cross-linking study on the quaternary structure of Escherichia coli DNA-binding protein NS (HU)
    • Losso MA, Pawlik RT, Canonaco MA, Gualerzi CO (1986) Proteins from the prokaryotic nucleoid. A protein-protein cross-linking study on the quaternary structure of Escherichia coli DNA-binding protein NS (HU). Eur J Biochem 155: 27-32
    • (1986) Eur J Biochem , vol.155 , pp. 27-32
    • Losso, M.A.1    Pawlik, R.T.2    Canonaco, M.A.3    Gualerzi, C.O.4
  • 24
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller JH (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 25
    • 0032805887 scopus 로고    scopus 로고
    • The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
    • Nooren IMA, Kaptein R, Sauer RT, Boelens R (1999) The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nat Struct Biol 6: 755-759
    • (1999) Nat Struct Biol , vol.6 , pp. 755-759
    • Nooren, I.M.A.1    Kaptein, R.2    Sauer, R.T.3    Boelens, R.4
  • 26
    • 28844466803 scopus 로고    scopus 로고
    • Repression of transcription by curved DNA and nucleoid protein H-NS: A mode of bacterial gene regulation
    • Ohyama T (ed). Austin: Landes Bioscience (in press)
    • Pon CL, Stella S, Gualerzi CO (2005) Repression of transcription by curved DNA and nucleoid protein H-NS: a mode of bacterial gene regulation. In DNA Conformation and Transcription, Ohyama T (ed). Austin: Landes Bioscience (in press)
    • (2005) DNA Conformation and Transcription
    • Pon, C.L.1    Stella, S.2    Gualerzi, C.O.3
  • 27
    • 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 JCD, Higgins CF, Driscoll PC, Ladbury JE (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
  • 28
    • 0025359664 scopus 로고
    • Sequence determinants for H1 binding on Escherichia coli lac and gal promoters
    • Rimsky S, Spassky A (1990) Sequence determinants for H1 binding on Escherichia coli lac and gal promoters. Biochemistry 29: 3765-3771
    • (1990) Biochemistry , vol.29 , pp. 3765-3771
    • Rimsky, S.1    Spassky, A.2
  • 31
    • 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, 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
  • 33
    • 0021760528 scopus 로고
    • H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro
    • Spassky A, Rimsky S, Garreau H, Buc H (1984) H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro. Nucleic Acids Res 12: 5321-5340
    • (1984) Nucleic Acids Res , vol.12 , pp. 5321-5340
    • Spassky, A.1    Rimsky, S.2    Garreau, H.3    Buc, H.4
  • 34
    • 0026573628 scopus 로고
    • Lethal overproduction of the Escherichia coli nucleoid protein H-NS: Ultramicroscopic and molecular autopsy
    • Spurio R, Durrenberger M, Falconi M, La Teana A, Pon CL, Gualerzi CO (1992) Lethal overproduction of the Escherichia coli nucleoid protein H-NS: ultramicroscopic and molecular autopsy. Mol Gen Genet 231: 201-211
    • (1992) Mol Gen Genet , vol.231 , pp. 201-211
    • Spurio, R.1    Durrenberger, M.2    Falconi, M.3    La Teana, A.4    Pon, C.L.5    Gualerzi, C.O.6
  • 35
    • 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 CL, Gualerzi CO (1997) The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J 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
  • 36
    • 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, 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
  • 37
    • 0030601826 scopus 로고    scopus 로고
    • Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS
    • Ueguchi C, Tomomi S, Yoshida 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    Tomomi, S.2    Yoshida, T.3
  • 39
    • 0029785418 scopus 로고    scopus 로고
    • Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using the dominant negative derivatives
    • Williams RM, Rimsky S, Buc H (1996) Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using the 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
  • 40
    • 0028234761 scopus 로고
    • Modulated expression of promoters containing upstream curved DNA sequences by the Escherichia coli nucleoid protein H-NS
    • Zuber F, Kotlarz D, Rimsky S, Bue H (1994) Modulated expression of promoters containing upstream curved DNA sequences by the Escherichia coli nucleoid protein H-NS. Mol Microbiol 12: 231-240
    • (1994) Mol Microbiol , vol.12 , pp. 231-240
    • Zuber, F.1    Kotlarz, D.2    Rimsky, S.3    Bue, H.4


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