Lloyd, Janice A.
Forget, Anthony L.
Knight, Kendall L.
Borgstahl, Gloria E. O.
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
KeywordsDNA Repair; DNA-Binding Proteins; Humans; Kinetics; Microscopy, Electron; Mutagenesis; Peptide Fragments; Recombinant Proteins; Sequence Deletion; Thioredoxins
Medicine and Health Sciences
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AbstractThe human RAD52 protein plays an important role in the earliest stages of chromosomal double-strand break repair via the homologous recombination pathway. Individual subunits of RAD52 self-associate into rings that can then form higher order complexes. RAD52 binds to double-strand DNA ends, and recent studies suggest that the higher order self-association of the rings promotes DNA end-joining. Earlier studies defined the self-association domain of RAD52 to a unique region in the N-terminal half of the protein. Here we show that there are in fact two experimentally separable self-association domains in RAD52. The N-terminal self-association domain mediates the assembly of monomers into rings, and the previously unidentified domain in the C-terminal half of the protein mediates higher order self-association of the rings.
SourceJ Biol Chem. 2001 May 11;276(19):15876-80. Epub 2001 Feb 13. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/33569
Related ResourcesLink to article in PubMed