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Interaction with Rad51 Is Indispensable for Recombination Mediator Function of Rad52
In the yeast Saccharomyces cerevisiae , the RAD52 gene is indispensable for homologous recombination and DNA repair. Rad52 protein binds DNA, anneals complementary ssDNA strands, and self-associates to form multimeric complexes. Moreover, Rad52 physically interacts with the Rad51 recombinase and ser...
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Published in: | The Journal of biological chemistry 2002-10, Vol.277 (42), p.40132-40141 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | In the yeast Saccharomyces cerevisiae , the RAD52 gene is indispensable for homologous recombination and DNA repair. Rad52 protein binds DNA, anneals complementary ssDNA strands,
and self-associates to form multimeric complexes. Moreover, Rad52 physically interacts with the Rad51 recombinase and serves
as a mediator in the Rad51-catalyzed DNA strand exchange reaction. Here, we examine the functional significance of the Rad51/Rad52
interaction. Through a series of deletions, we have identified residues 409â420 of Rad52 as being indispensable and likely
sufficient for its interaction with Rad51. We have constructed a four-amino acid deletion mutation within this region of Rad52
to ablate its interaction with Rad51. We show that the rad52Î409â412 mutant protein is defective in the mediator function
in vitro even though none of the other Rad52 activities, namely, DNA binding, ssDNA annealing, and protein oligomerization, are affected.
We also show that the sensitivity of the rad52Î409â412 mutant to ionizing radiation can be complemented by overexpression of Rad51. These results thus demonstrate the significance
of the Rad51-Rad52 interaction in homologous recombination. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M206511200 |