Kinetic analysis of operator binding by the E coli methionine repressor highlights the role(s) of electrostatic interactions

被引：10

作者：

Lawrenson, ID ^{[1
]}

Stockley, PG ^{[1
]}

机构：

[1] Univ Leeds, Astbury Ctr Struct Mol Biol, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

FEBS LETTERS | 2004年 / 564卷 / 1-2期

基金：

英国生物技术与生命科学研究理事会;

关键词：

methionine repressor; operator binding; surface plasmon resonance; Escherichia coli;

D O I：

10.1016/S0014-5793(04)00336-9

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：

MetJ is a member of the ribbon-helix-helix class of DNA-binding proteins whose affinity for operators is apparently controlled by an unprecedented long-range electrostatic effect from the tertiary sulphur atom of its co-repressor, S-adenosyl methionine. We report here the results of kinetic assays of DNA binding with MetJ mutant proteins having altered net charges. The results (a) suggest that MetJ locates its operators via a sliding mechanism, (b) support the idea that electrostatic steering is important in the initial DNA binding event and (c) highlight the sensitivity of this system to electrostatic effects. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：136 / 142

页数：7

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