Amino-terminal domain interactions of λ integrase on arm-type DNA

被引：1
|
作者：
Lee, Sang Yeol [1 ]
机构：
[1] Kyungwon Univ, Dept Life Sci, Songnam 461701, Kyeonggi Do, South Korea
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 376卷 / 01期
关键词：
protein-DNA interactions; protein-protein interactions; multimeric complexes; site-specific DNA recombination;
D O I：
10.1016/j.bbrc.2008.08.109
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
In contrast to the other tyrosine recombinase family members, integrase protein (Int) of bacteriophage lambda has an additional amino-terminal domain that binds to "arm-type" DNA sequences distant from those involved in strand exchange. The homomeric interaction between neighboring amino-terminal domains of Int is contributed by R30-D71 salt-bridge in a non-equivalent manner on Holliday-junction intermediates. In this report, R30 and D71 residues were investigated in regard to Int's cooperative binding to "arm-type" DNA and the attenuating function of "arm-type" DNA. The results suggest the electrostatic interaction between residues 30 and 71 is dependent on "arm-type" DNA and contributes the "selective" inhibition of catalytic activity of lambda Int by "arm-type" DNA. (C) 2008 Elsevier Inc. All rights reserved.
引用
收藏
页码：139 / 142
页数：4
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