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Biochimie. 2001 Feb;83(2):231-4.

Structural basis for preferential binding of H-NS to curved DNA.

Author information

1
Laboratory of Molecular Genetics, Gorlaeus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, The Netherlands.

Abstract

The Escherichia coli H-NS protein is a nucleoid-associated protein involved in transcription regulation and DNA compaction. H-NS exerts its role in DNA condensation by non-specific interactions with DNA. With respect to transcription regulation preferential binding sites in the promoter regions of different genes have been reported. In this paper we describe the analysis of H-NS-DNA complexes on a preferred H-NS binding site by atomic force microscopy. On the basis of these data we present a model for the specific recognition of DNA by H-NS as a function of DNA curvature.

PMID:
11278073
DOI:
10.1016/s0300-9084(00)01213-x
[Indexed for MEDLINE]

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