A molecular mechanism for the repression of transcription by the H-NS protein
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作者:
Rimsky, S
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Inst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, FranceInst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, France
Rimsky, S
[1
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Zuber, F
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Inst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, FranceInst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, France
Zuber, F
[1
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Buckle, M
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Inst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, FranceInst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, France
Buckle, M
[1
]
Buc, H
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Inst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, FranceInst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, France
Buc, H
[1
]
机构:
[1] Inst Pasteur, Unite Physicochim Macromol Biol, CNRS, URA 1773, F-75724 Paris 15, France
The H-NS protein is a major component of the bacterial nucleoid and plays a crucial role in the global gene regulation of enteric bacteria. Although H-NS does not exhibit a high DNA sequence specificity, a number of H-NS-responsive promoters have been shown to contain regions of intrinsic DNA curvature located either upstream or downstream of the transcription start point. We have studied H-NS binding to DNA and in vitro transcriptional regulation by H-NS at several synthetic promoters with or without curved sequences inserted upstream of the Pribnow box. We show how such inserts determine the final organization of H-NS-containing nucleoprotein complexes and how this affects transcription. We refine a two-step mechanism for the constitution of H-NS assemblies that are efficient in regulation.