Complex formation by the human RAD51C and XRCC3 recombination repair proteins
Author(s) -
JeanYves Masson,
Alicja Z. Stasiak,
Andrzej Stasiak,
Fiona E. Benson,
Stephen C. West
Publication year - 2001
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.111005698
Subject(s) - xrcc3 , rad51 , biology , dna repair , dna , replication protein a , microbiology and biotechnology , homologous recombination , genetics , genetic recombination , gene , recombination , dna binding protein , genotype , single nucleotide polymorphism , transcription factor
In vertebrates, the RAD51 protein is required for genetic recombination, DNA repair, and cellular proliferation. Five paralogs of RAD51, known as RAD51B, RAD51C, RAD51D, XRCC2, and XRCC3, have been identified and also shown to be required for recombination and genome stability. At the present time, however, very little is known about their biochemical properties or precise biological functions. As a first step toward understanding the roles of the RAD51 paralogs in recombination, the human RAD51C and XRCC3 proteins were overexpressed and purified from baculovirus-infected insect cells. The two proteins copurify as a complex, a property that reflects their endogenous association observed in HeLa cells. Purified RAD51C--XRCC3 complex binds single-stranded, but not duplex DNA, to form protein--DNA networks that have been visualized by electron microscopy.
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