Abstract
The yeast RAD52 protein is required for both homologous DNA recombination and repair of DNA double-strand breaks. RAD52 can bind to the yeast RAD51 protein, which shares a functional similarity with the bacterial RecA protein. The gene encoding the human homolog of the yeast RAD52 protein shares significant N-terminus amino acid homology with the yeast RAD52 protein. Using a yeast two hybrid system and purified GST-RAD52 fusion protein, we demonstrate that the human RAD52 protein self-associates both in vivo and in vitro. The region of RAD52 required for its self-interaction, mapped here as amino acid residues 65-165, has significant homology with the yeast RAD52 (52% identity, and 89% similarity), suggesting the importance of self-association for RAD52's function.
Original language | English (US) |
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Pages (from-to) | 81-89 |
Number of pages | 9 |
Journal | Mutation Research - DNA Repair |
Volume | 364 |
Issue number | 2 |
DOIs | |
State | Published - Oct 18 1996 |
Keywords
- DNA double-strand breaks
- DSB
- RAD51
- RAD52
- Two hybrid system
ASJC Scopus subject areas
- Molecular Biology
- Toxicology
- Genetics