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phiC31整合酶N端结构域在attB-attP联会中的作用

Role of the N-terminal domain of phiC31 integrase in attB-attP synapsis.

作者信息

Rowley Paul A, Smith Margaret C M

机构信息

Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.

出版信息

J Bacteriol. 2008 Oct;190(20):6918-21. doi: 10.1128/JB.00612-08. Epub 2008 Aug 8.

Abstract

PhiC31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.

摘要

PhiC31整合酶是一种丝氨酸重组酶,包含一个提供催化活性的N端结构域(NTD)和一个控制哪一对DNA底物能够发生联会的大的C端结构域。我们在此表明,NTD中氨基酸V129的替换可导致联会和DNA切割缺陷,这表明NTD在联会中也具有重要作用。

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本文引用的文献

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