NMR Analysis of the Architecture and Functional Remodeling of a Modular Multidomain Protein, RPA

被引：39

作者：

Brosey, Chris A.

Chagot, Marie-Eve

Ehrhardt, Mark

Pretto, Dalyir I.

Weiner, Brian E.

Chazin, Walter J. ^{[1
]}

机构：

[1] Vanderbilt Univ, Dept Biochem, Nashville, TN 37232 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 18期

关键词：

A PHOSPHORYLATION; CELL-CYCLE; REPLICATION; BINDING; DOMAIN;

D O I：

10.1021/ja9013634

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Modular proteins with multiple domains tethered by flexible linkers have variable global architectures. Using the eukaryotic ssDNA binding protein, Replication Protein A (RPA), we demonstrate that NMR spectroscopy is a powerful tool to characterize the remodeling of architecture in different functional states. The first direct evidence is obtained for the remodeling of RPA upon binding ssDNA, including an alteration in the availability of the RPA32N domain that may help explain its damage-dependent phosphorylation.

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页码：6346 / +

页数：3

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