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大肠杆菌膜对半甲基化oriC的高亲和力结合是由一个多蛋白系统介导的,该系统包括SeqA和一个新鉴定的因子SeqB。

High-affinity binding of hemimethylated oriC by Escherichia coli membranes is mediated by a multiprotein system that includes SeqA and a newly identified factor, SeqB.

作者信息

Shakibai N, Ishidate K, Reshetnyak E, Gunji S, Kohiyama M, Rothfield L

机构信息

Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06032, USA.

出版信息

Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11117-21. doi: 10.1073/pnas.95.19.11117.

Abstract

The binding of hemimethylated oriC to Escherichia coli membranes has been implicated in the prevention of premature reinitiation at newly replicated chromosomal origins in a reaction that involves the SeqA protein. We describe the resolution of the membrane-associated oriC-binding activity into two fractions, both of which are required for the high-affinity binding of hemimethylated oriC. The active component in one fraction is identified as SeqA. The active component of the second fraction is a previously undescribed protein factor, SeqB. The reconstituted system reproduced the salient characteristics of the membrane-associated binding activity, suggesting that the membrane-associated oriC-binding machinery of E. coli is likely to be a multiprotein system that includes the SeqA and SeqB proteins.

摘要

半甲基化的oriC与大肠杆菌细胞膜的结合被认为参与了在一个涉及SeqA蛋白的反应中防止新复制的染色体起始位点过早重新起始。我们描述了将与膜相关的oriC结合活性解析为两个组分,这两个组分对于半甲基化oriC的高亲和力结合都是必需的。一个组分中的活性成分被鉴定为SeqA。第二个组分的活性成分是一种先前未描述的蛋白质因子,SeqB。重组系统重现了与膜相关的结合活性的显著特征,这表明大肠杆菌的与膜相关的oriC结合机制可能是一个包括SeqA和SeqB蛋白的多蛋白系统。

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