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PMID: 8879274 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Self-association of human RAD52 protein.

Mutation research ·Vol. 364 ·No. 2 ·1996-10-18 ·Pages 81-9

Shen Z, Peterson SR, Comeaux JC, Zastrow D, Moyzis RK, Bradbury EM, Chen DJ

Abstract

The yeast RAD52 protein is required for both homologous DNA recombination and repair of DNA double-strand breaks. RAD52 can bind to the yeast RAD51 protein, which shares a functional similarity with the bacterial RecA protein. The gene encoding the human homolog of the yeast RAD52 protein shares significant N-terminus amino acid homology with the yeast RAD52 protein. Using a yeast two hybrid system and purified GST-RAD52 fusion protein, we demonstrate that the human RAD52 protein self-associates both in vivo and in vitro. The region of RAD52 required for its self-interaction, mapped here as amino acid residues 65-165, has significant homology with the yeast RAD52 (52% identity, and 89% similarity), suggesting the importance of self-association for RAD52's function.

MeSH Terms
Binding Sites DNA Damage DNA Repair DNA-Binding Proteins/genetics,metabolism Fungal Proteins/genetics,metabolism Humans Protein Binding Protein Conformation Rad51 Recombinase Recombinant Fusion Proteins/metabolism
Chemicals
DNA-Binding Proteins Fungal Proteins Recombinant Fusion Proteins RAD51 protein, human Rad51 Recombinase
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Shen Z
Life Sciences Division, Los Alamos National Laboratory, NM 87545, USA.
Peterson S R
Comeaux J C
Zastrow D
Moyzis R K
Bradbury E M
Chen D J
Article Info
Journal
Mutation research
Abbr.
Mutat Res
ISSN
0027-5107
Published
1996-10-18
Pages
81-9
Language
English
Region
Netherlands
NLM ID
0400763
Subset
IM
Grants
NCI NIH HHS · CA50519 · United States
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