Abstract
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.
Original language | English (US) |
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Pages (from-to) | 15876-15880 |
Number of pages | 5 |
Journal | Journal of Biological Chemistry |
Volume | 276 |
Issue number | 19 |
DOIs | |
State | Published - May 11 2001 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology