PMID:11278073

Citation	Dame, RT, Wyman, C and Goosen, N (2001) Structural basis for preferential binding of H-NS to curved DNA. Biochimie 83:231-4
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.
Links	PubMed
Keywords	Bacterial Proteins/metabolism; Bacterial Proteins/ultrastructure; DNA Primers/chemistry; DNA, Bacterial/metabolism; DNA, Bacterial/ultrastructure; DNA-Binding Proteins/metabolism; DNA-Binding Proteins/ultrastructure; Escherichia coli; Microscopy, Atomic Force; Nucleic Acid Conformation; Polymerase Chain Reaction; Protein Binding; Protein Conformation
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