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PMID: 15141025 Published · epublish English Journal Article Research Support, Non-U.S. Gov't

Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex.

Nucleic acids research ·Vol. 32 ·No. 8 ·2004-00-00 ·Pages 2556-65

Yokoyama H, Sarai N, Kagawa W, Enomoto R, Shibata T, Kurumizaka H, Yokoyama S

Abstract

The Rad51B, Rad51C, Rad51D and Xrcc2 proteins are Rad51 paralogs, and form a complex (BCDX2 complex) in mammalian cells. Mutant cells defective in any one of the Rad51-paralog genes exhibit spontaneous genomic instability and extreme sensitivity to DNA-damaging agents, due to inefficient recombinational repair. Therefore, the Rad51 paralogs play important roles in the maintenance of genomic integrity through recombinational repair. In the present study, we examined the DNA-binding preference of the human BCDX2 complex. Competitive DNA-binding assays using seven types of DNA substrates, single-stranded DNA (ssDNA), double-stranded DNA, 5'- and 3'-tailed duplexes, nicked duplex DNA, Y-shaped DNA and a synthetic Holliday junction, revealed that the BCDX2 complex preferentially bound to the two DNA substrates with branched structures (the Y-shaped DNA and the synthetic Holliday junction). Furthermore, the BCDX2 complex catalyzed the strand-annealing reaction between a long linear ssDNA (1.2 kb in length) and its complementary circular ssDNA. These properties of the BCDX2 complex may be important for its roles in the maintenance of chromosomal integrity.

MeSH Terms
Adenosine Triphosphatases/metabolism Binding Sites DNA/chemistry,metabolism DNA, Cruciform/metabolism DNA, Single-Stranded/metabolism DNA-Binding Proteins/metabolism Macromolecular Substances Nucleic Acid Conformation
Chemicals
DNA, Cruciform DNA, Single-Stranded DNA-Binding Proteins Macromolecular Substances RAD51B protein, human RAD51C protein, human RAD51D protein, human XRCC2 protein, human DNA Adenosine Triphosphatases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Yokoyama Hiroshi
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Sarai Naoyuki
Kagawa Wataru
Enomoto Rima
Shibata Takehiko
Kurumizaka Hitoshi
Yokoyama Shigeyuki
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
DOI
10.1093/nar/gkh578
Published
2004-00-00
Epub
2004-00-11
Pages
2556-65
Language
English
Region
England
NLM ID
0411011
PMCID
PMC419466
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/gkh578 PMC Full Text View journal details
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