Dame R T, Wyman C, Goosen N
Laboratory of Molecular Genetics, Gorlaeus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, The Netherlands.
Biochimie. 2001 Feb;83(2):231-4. doi: 10.1016/s0300-9084(00)01213-x.
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.
大肠杆菌H-NS蛋白是一种与类核相关的蛋白，参与转录调控和DNA压缩。H-NS通过与DNA的非特异性相互作用在DNA凝聚中发挥作用。关于转录调控，已报道了不同基因启动子区域中的优先结合位点。在本文中，我们描述了通过原子力显微镜对H-NS与一个优先的H-NS结合位点上的DNA复合物的分析。基于这些数据，我们提出了一个模型，用以说明H-NS对DNA的特异性识别是DNA曲率的函数。
