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

Abstract:

: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 A. 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.

authors

Singleton MR,Wentzell LM,Liu Y,West SC,Wigley DB

doi

10.1073/pnas.212449899

keywords:

subject

Has Abstract

pub_date

2002-10-15 00:00:00

pages

13492-7

issue

21

eissn

0027-8424

issn

1091-6490

pii

212449899

journal_volume

99

pub_type

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