Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 321, Issue 1, Pages 133-148Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(02)00541-7
Keywords
human Rad52; replication protein A; double-strand break repair; protein-protein interaction; single-stranded DNA binding
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Funding
- NIGMS NIH HHS [R01-GM44721] Funding Source: Medline
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The eukaryotic single-stranded DNA-binding protein, replication protein DNA repair and DNA recombination. Rad52 and RPA, along with other members of the Rad52 epistasis group of genes, repair double-stranded DNA breaks (DSBs). Two repair pathways involve RPA and Rad52, homologous recombination and single-strand annealing. Two binding sites for Rad52 have been identified on RPA. They include the previously, identified C-terminal domain (CTD) of RPA32 (residues 224-271) and the newly identified domain containing residues 169-326 of RPA70. A region on Rad52, which includes residues 218-303, binds RPA70 as well as RPA32. The N-terminal region of RPA32 does not appear to play a role in the formation of the RPA:Rad52 complex. It appears that the RPA32CTD can substitute for RPA70 in binding Rad52. Sequence homology between RPA32 and RPA70 was used to identify a putative Rad52-binding site on RPA70 that is located near DNA-binding domains A and B. Rad52 binding to RPA increases ssDNA affinity significantly. Mutations in DBD-D on RPA32 show that this domain is primarily responsible for the ssDNA binding enhancement. RPA binding to Rad52 inhibits the higher-order self-association of Rad52 rings. Implications for these results for the hand-off mechanism between protein-protein partners, including Rad51, in homologous recombination and single-strand annealing are discussed. (C) 2002 Elsevier Science Ltd. All rights reserved.
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