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DNA与DNA结合蛋白的相互作用。II. 大肠杆菌DNA解旋蛋白的置换以及与蛋白HD复合的DNA的凝聚结构

Interaction of DNA with DNA binding proteins. II. Displacement of Escherichia coli DNA unwinding protein and the condensed structure of DNA complexed with protein HD.

作者信息

Zentgraf H, Berthold V, Geider K

出版信息

Biochim Biophys Acta. 1977 Feb 16;474(4):629-38. doi: 10.1016/0005-2787(77)90082-x.

DOI:10.1016/0005-2787(77)90082-x
PMID:319835
Abstract

Three DNA binding proteins from Escherichia coli cells have been complexed with single-stranded phage fd DNA. Electron microscopy reveals granular substructures in the complexes formed with protein HD. In complexes of DNA unwinding protein with fd DNA both protein HD and phage-coded gene 5 protein partially displace the unwinding protein which results in the formation of structures characteristic for the DNA complexes formed with either protein HD or gene 5 protein alone. Combination of protein HD with double-stranded phage T7 DNA leads to a progressive folding and condensing of the genome. The structures observed are discussed in relation to current concepts of the packing of DNA in protein complexes.

摘要

来自大肠杆菌细胞的三种DNA结合蛋白已与单链噬菌体fd DNA形成复合物。电子显微镜显示,与蛋白质HD形成的复合物中有颗粒状亚结构。在解旋蛋白与fd DNA的复合物中,蛋白质HD和噬菌体编码的基因5蛋白都会部分取代解旋蛋白,从而导致形成与单独与蛋白质HD或基因5蛋白形成的DNA复合物特有的结构。蛋白质HD与双链噬菌体T7 DNA结合会导致基因组逐渐折叠和浓缩。结合当前关于DNA在蛋白质复合物中包装的概念,对观察到的结构进行了讨论。

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