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Genes Dev. 2010 Feb 15;24(4):339-44. doi: 10.1101/gad.1883510.

A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes.

Author information

1
Department of Physics, National University of Singapore, Singapore 117542.

Abstract

Heat-stable nucleoid structuring protein (H-NS) is an abundant prokaryotic protein that plays important roles in organizing chromosomal DNA and gene silencing. Two controversial binding modes were identified. H-NS binding stimulating DNA bridging has become the accepted mechanism, whereas H-NS binding causing DNA stiffening has been largely ignored. Here, we report that both modes exist, and that changes in divalent cations drive a switch between them. The stiffening form is present under physiological conditions, and directly responds to pH and temperature in vitro. Our findings have broad implications and require a reinterpretation of the mechanism by which H-NS regulates genes.

PMID:
20159954
PMCID:
PMC2816733
DOI:
10.1101/gad.1883510
[Indexed for MEDLINE]
Free PMC Article

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