Human RAD52 exhibits two modes of self-association.
The 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.
Department of Chemistry, University of Toledo, Toledo, Ohio 43606-3390, USA.
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D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D006801:Humans; D007700:Kinetics; D008854:Microscopy, Electron; D016296:Mutagenesis; D010446:Peptide Fragments / Q000737:chemistry / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D017384:Sequence Deletion; D013879:Thioredoxins / Q000737:chemistry / Q000378:metabolism
D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D013879:Thioredoxins