New insight into mediator function of yeast Rad52 protein

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Authors

KREJCI Lumir PLATE Iben SUNG Patrick SEHORN Michael BUSSEN Wendy MORTENSEN Uffe H.

Year of publication 2005
Type Article in Proceedings
Conference XXIIth International Conference on Yeast Genetics and Molecular Biology
MU Faculty or unit

Faculty of Science

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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