与细菌RecA蛋白一同运转。

Motoring along with the bacterial RecA protein.

作者信息

Cox Michael M

机构信息

Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, Wisconsin 53706-1544, USA.

出版信息

Nat Rev Mol Cell Biol. 2007 Feb;8(2):127-38. doi: 10.1038/nrm2099. Epub 2007 Jan 17.

DOI:10.1038/nrm2099

PMID:17228330

Abstract

The recombinases of the RecA family are often viewed only as DNA-pairing proteins - they bind to one DNA segment, align it with homologous sequences in another DNA segment, promote an exchange of DNA strands and then dissociate. To a first approximation, this description seems to fit the eukaryotic (Rad51 and Dmc1) and archaeal (RadA) RecA homologues. However, the bacterial RecA protein does much more, coupling ATP hydrolysis with DNA-strand exchange in a manner that greatly expands its repertoire of activities. This article explores the protein activities and experimental results that have identified RecA as a motor protein.

摘要

RecA家族的重组酶通常仅被视为DNA配对蛋白——它们与一个DNA片段结合，使其与另一个DNA片段中的同源序列对齐，促进DNA链的交换，然后解离。初步看来，这种描述似乎适用于真核生物（Rad51和Dmc1）和古细菌（RadA）的RecA同源物。然而，细菌RecA蛋白的功能要多得多，它将ATP水解与DNA链交换耦合在一起，从而极大地扩展了其活性范围。本文探讨了那些将RecA鉴定为一种分子马达蛋白的蛋白质活性和实验结果。