与hix位点复合的Hin重组酶DNA结合结构域中假定识别螺旋的方向。

Orientation of the putative recognition helix in the DNA-binding domain of Hin recombinase complexed with the hix site.

作者信息

Mack D P, Sluka J P, Shin J A, Griffin J H, Simon M I, Dervan P B

机构信息

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.

出版信息

Biochemistry. 1990 Jul 17;29(28):6561-7. doi: 10.1021/bi00480a003.

DOI:10.1021/bi00480a003

PMID:2204416

Abstract

On the basis of sequence similarity with other known DNA-binding proteins, the DNA-binding domain of Hin recombinase, residues 139-190, is thought to bind DNA by a helix-turn-helix motif. Two models can be considered that differ in the orientation of the recognition helix in the major groove of DNA. One is based on the orientation of the recognition helix found in the 434 repressor (1-69) and lambda repressor-DNA cocrystals, and the other is based on the NMR studies of lac repressor headpiece. Cleavage by EDTA.Fe attached to a lysine side chain (Ser183----Lys183) near the COOH terminus of Hin(139-184) reveals that the putative recognition helix is oriented toward the center of the inverted repeats in a manner similar to that seen in the 434 and lambda repressor-DNA cocrystals.

摘要

基于与其他已知DNA结合蛋白的序列相似性，Hin重组酶的DNA结合结构域（第139 - 190位氨基酸残基）被认为通过螺旋-转角-螺旋基序与DNA结合。可以考虑两种模型，它们在识别螺旋于DNA大沟中的方向上有所不同。一种基于在434阻遏蛋白（1 - 69）和λ阻遏蛋白-DNA共晶体中发现的识别螺旋方向，另一种基于乳糖阻遏蛋白头部的核磁共振研究。通过连接到Hin（139 - 184）COOH末端附近赖氨酸侧链（Ser183→Lys183）上的EDTA.Fe进行切割，结果表明推定的识别螺旋以类似于在434和λ阻遏蛋白-DNA共晶体中观察到的方式朝向反向重复序列的中心。