Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 5, Pages 441-448Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1233
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Funding
- Medical Research Council [MC_U105184288] Funding Source: Medline
- MRC [MC_U105184288] Funding Source: UKRI
- Medical Research Council [MC_U105184288] Funding Source: researchfish
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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.
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