A divalent metal-mediated switch controlling protein-induced DNA bending

被引:15
作者
Bao, Qiuye
Chen, Hu
Liu, Yingjie
Yan, Jie
Droge, Peter
Davey, Curt A.
机构
[1] Nanyang Technol Univ, Sch Biol Sci, Div Genom & Genet, Singapore 637551, Singapore
[2] Natl Univ Singapore, Dept Phys, Singapore 117542, Singapore
[3] Nanyang Technol Univ, Sch Biol Sci, Div Struct & Computat Biol, Singapore 637551, Singapore
基金
澳大利亚研究理事会;
关键词
divalent metal; DNA architectural proteins; DNA topology; integration host factor; nucleoprotein complex formation;
D O I
10.1016/j.jmb.2006.09.082
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
Architectural proteins that reconfigure the paths of DNA segments are required for the establishment of functional interfaces in many genomic transactions. A single-chain derivative of the DNA architectural protein integration host factor was found to adopt two stable conformational states in complex with a specific DNA target. In the so-called open state, the degree of protein-induced DNA bending is reduced significantly compared with the closed state. The conformational switch between these states is controlled by divalent metal binding in two electronegative zones arising from the lysine-to-glutamate substitution in the protein body proximal to the phosphate backbone of one DNA arm. We show that this switch can be employed to control the efficiency of site-specific recombination catalyzed by X integrase. Introduction of acidic residues at the protein-DNA interface holds potential for the design of metal-mediated switches for the investigation of functional relationships. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码:731 / 740
页数:10
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