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Papers In Press, published online ahead of print June 27, 2000
ICRF, Institute of Molecular Medicine, Oxford, Oxon OX3 7DN
Corresponding Author: i.hickson{at}icrf.icnet.uk
The Rad51 protein in eukaryotic cells is a structural and functional homolog of E.coli RecA with a role in DNA repair and genetic recombination. Several proteins showing sequence similarity to Rad51 have previously been identified in both yeast and human cells. In S. cerevisiae, two of these proteins, Rad55p and Rad57p, form a heterodimer that can stimulate Rad51-mediated DNA strand exchange. Here, we report the purification of one of the representatives of the RAD51 family in human cells. We demonstrate that the purified RAD51L3 protein possesses single-stranded DNA binding activity and DNA-stimulated ATPase activity, consistent with the presence of 'Walker-box' motifs in the deduced RAD51L3 sequence. We have identified a protein complex in human cells containing RAD51L3 and a second RAD51 family member, XRCC2. Using purified proteins, we demonstrate that the interaction between RAD51L3 and XRCC2 is direct. Given the requirements for XRCC2 in genetic recombination and protection against DNA damaging agents, we suggest that the complex of RAD51L3 and XRCC2 is likely to be important for these functions in human cells.
J. Biol. Chem, 10.1074/jbc.M002075200
Submitted on March 13, 2000
Revised on June 22, 2000
Accepted on June 26, 2000
The RAD51 Family Member, RAD51L3, is a DNA-stimulated ATPase that Forms a Complex with XRCC2
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