Journal
MOLECULAR CELL
Volume 67, Issue 1, Pages 19-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2017.05.019
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Funding
- National Cancer Institute of the NIH [CA188347, P30CA056036]
- Drexel Coulter Program Award
- National Institute of General Medical Sciences (NIGMS) of the NIH [GM115927]
- National Science Foundation [1615335]
- Howard Hughes Medical Institute Faculty Scholar [55108574]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1615335] Funding Source: National Science Foundation
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RNA can serve as a template for DNA double-strand break repair in yeast cells, and Rad52, a member of the homologous recombination pathway, emerged as an important player in this process. However, the exact mechanism of how Rad52 contributes to RNA-dependent DSB repair remained unknown. Here, we report an unanticipated activity of yeast and human Rad52: inverse strand exchange, in which Rad52 forms a complex with dsDNA and promotes strand exchange with homologous ssRNA or ssDNA. We show that in eukaryotes, inverse strand exchange between homologous dsDNA and RNA is a distinctive activity of Rad52; neither Rad51 recombinase nor the yeast Rad52 paralog Rad59 has this activity. In accord with our in vitro results, our experiments in budding yeast provide evidence that Rad52 inverse strand exchange plays an important role in RNA-templated DSB repair in vivo.
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