Structure of the single-strand annealing domain of human RAD52 protein

被引：186

作者：

Singleton, MR ^{[1
]}

Wentzell, LM ^{[1
]}

Liu, YL ^{[1
]}

West, SC ^{[1
]}

Wigley, DB ^{[1
]}

机构：

[1] Canc Res UK, London Res Ins, Clare Hall Labs, S Mimms EN6 3LD, Herts, England

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2002年 / 99卷 / 21期

关键词：

recombination; DNA repair; crystallography;

D O I：

10.1073/pnas.212449899

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In eukaryotic cells, RAD52 protein plays a central role in genetic recombination and DNA repair by (i) promoting the annealing of complementary single-stranded DNA and (ii) stimulation of the RAD51 recombinase. The single-strand annealing domain resides in the N-terminal region of the protein and is highly conserved, whereas the nonconserved RAD51-interaction domain is located in the C-terminal region. An N-terminal fragment of human RAD52 (residues 1-209) has been purified to homogeneity and, similar to the full-size protein (residues 1-418), shown to promote single-strand annealing in vitro. We have determined the crystal structure of this single-strand annealing domain at 2.7 Angstrom. The structure reveals an undecameric (11) subunit ring with extensive subunit contacts. A large, positively charged groove runs along the surface of the ring, readily suggesting a mechanism by which RAD52 presents the single strand for reannealing with complementary single-stranded DNA.

引用

页码：13492 / 13497

页数：6

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