TetR和CAP中的相反变构机制。
Opposite allosteric mechanisms in TetR and CAP.
作者信息
Seedorff Jennifer E, Rodgers Michael E, Schleif Robert
机构信息
Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.
出版信息
Protein Sci. 2009 Apr;18(4):775-81. doi: 10.1002/pro.88.
Abstract
Regulation of the DNA binding affinity of an oligomeric protein can be considered to consist of an intrinsic component, in which the affinity of an individual DNA-binding domain is modulated in response to effector binding, and an extrinsic component, in which the relative position of the protein's two DNA-binding domains are altered so that they can or cannot contact both half-site operators simultaneously. We demonstrated directly that the TetR repressor utilizes an extrinsic mechanism and CAP, the catabolite activator protein, utilizes an intrinsic mechanism.
摘要
寡聚蛋白的DNA结合亲和力调控可被认为由内在成分和外在成分组成。内在成分中，单个DNA结合结构域的亲和力会响应效应物结合而被调节；外在成分中，蛋白质两个DNA结合结构域的相对位置发生改变，使得它们能够或无法同时与两个半位点操纵子接触。我们直接证明了TetR阻遏蛋白利用外在机制，而分解代谢物激活蛋白CAP利用内在机制。
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