H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing

被引:207
作者
Bouffartigues, Emeline
Buckle, Malcolm
Badaut, Cyril
Travers, Andrew
Rimsky, Sylvie
机构
[1] Ecole Normale Super, LBPA, UMR 8113, CNRS, F-94235 Cachan, France
[2] Fac Pharm Paris 5, IRD, F-75006 Paris, France
[3] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
基金
英国医学研究理事会;
关键词
D O I
10.1038/nsmb1233
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
H-NS is a protein of the bacterial nucleoid involved in DNA compaction and transcription regulation. In vivo, H-NS selectively silences specific genes of the bacterial chromosome. However, many studies have concluded that H-NS binds sequence-independently to DNA, leaving the molecular basis for its selectivity unexplained. We show that the negative regulatory element (NRE) of the supercoiling-sensitive Escherichia coli proU gene contains two identical high-affinity binding sites for H-NS. Cooperative binding of H-NS is abrogated by changes in DNA superhelical density and temperature. We further demonstrate that the high-affinity sites nucleate cooperative binding and establish a nucleoprotein structure required for silencing. Mutations in these sites result in loss of repression by H-NS. In this model, silencing at proU, and by inference at other genes directly regulated by H-NS, is tightly controlled by the cooperativity between bound H-NS molecules.
引用
收藏
页码:441 / 448
页数:8
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