New insight into mediator function of yeast Rad52 protein
| Authors | |
|---|---|
| Year of publication | 2005 |
| Type | Article in Proceedings |
| Conference | XXIIth International Conference on Yeast Genetics and Molecular Biology |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.yeast2005.org/ |
| Field | Biochemistry |
| Keywords | Recombination; DNA repair; Rad52; mediator; yeast |
| Description | Homologous recombination (HR) represents an important means for the repair of chromosome breaks induced by exogenous agents (e.g. ionizing radiation) or that arise endogenously (e.g. replication of a damaged DNA template). The elimination of these breaks is critical for the maintenance of genome stability. DNA strand break repair by HR is mediated by genes of the RAD52 epistasis group, whose structure and function are highly conserved among eukaryotes. Rad52 protein plays central role in this process. It binds and anneals complemtary ssDNA, self-associate to form multimeric rings, interacts with Rad51, and promotes nucleation of Rad51 onto ssDNA. Here, we show that Rad52 contains second DNA binding domain that is capable of mediating Rad51-catalyzed strand exchange reaction. The molecular mechanism of Rad52 function in homologous recombination is disccused. |
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