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Complex Formation by the Human RAD51C and XRCC3 Recombination Repair Proteins
Jean-Yves Masson, Alicja Z. Stasiak, Andrzej Stasiak, Fiona E. Benson and Stephen C. West
Proceedings of the National Academy of Sciences of the United States of America
Vol. 98, No. 15 (Jul. 17, 2001), pp. 8440-8446
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3056188
Page Count: 7
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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 baculovirusinfected 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.
Proceedings of the National Academy of Sciences of the United States of America © 2001 National Academy of Sciences