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Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A

Author

Listed:
  • James H. New

    (Sections of Microbiology and of Molecular and Cellular Biology, University of California at Davis)

  • Tomohiko Sugiyama

    (Sections of Microbiology and of Molecular and Cellular Biology, University of California at Davis)

  • Elena Zaitseva

    (Sections of Microbiology and of Molecular and Cellular Biology, University of California at Davis)

  • Stephen C. Kowalczykowski

    (Sections of Microbiology and of Molecular and Cellular Biology, University of California at Davis)

Abstract

The generation of a double-strand break in the Saccharomyces cerevisiae genome is a potentially catastrophic event that can induce cell-cycle arrest or ultimately result in loss of cell viability.The repair of such lesions is strongly dependent on proteins encoded by the RAD52 epistasis group of genes (RAD50-55, RAD57, MRE11, XRS2)1,2, as well as the RFA13,4 and RAD59 genes5. rad52 mutants exhibit the most severe phenotypic defects in double-strand break repair2, but almost nothing is known about the biochemical role of Rad52 protein. Rad51 protein promotes DNA strand exchange6,7,8 and acts similarly to RecA protein9. Yeast Rad52 protein interacts with Rad51 protein10,11, binds single-stranded DNA and stimulates annealing of complementary single-stranded DNA12. We find that Rad52 protein stimulates DNA strand exchange by targeting Rad51 protein to a complex of replication protein A (RPA) with single-stranded DNA. Rad52 protein affects an early step in the reaction, presynaptic filament formation, by overcoming the inhibitory effects of the competitor, RPA. Furthermore, stimulation is dependent on the concerted action of both Rad51 protein and RPA, implying that specific protein–protein interactions between Rad52 protein, Rad51 protein and RPA are required.

Suggested Citation

  • James H. New & Tomohiko Sugiyama & Elena Zaitseva & Stephen C. Kowalczykowski, 1998. "Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A," Nature, Nature, vol. 391(6665), pages 407-410, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6665:d:10.1038_34950
    DOI: 10.1038/34950
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    Cited by:

    1. Jiawei Ding & Xiangting Li & Jiangchuan Shen & Yiling Zhao & Shuchen Zhong & Luhua Lai & Hengyao Niu & Zhi Qi, 2023. "ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Guangxue Liu & Jimin Li & Boxue He & Jiaqi Yan & Jingyu Zhao & Xuejie Wang & Xiaocong Zhao & Jingyan Xu & Yeyao Wu & Simin Zhang & Xiaoli Gan & Chun Zhou & Xiangpan Li & Xinghua Zhang & Xuefeng Chen, 2023. "Bre1/RNF20 promotes Rad51-mediated strand exchange and antagonizes the Srs2/FBH1 helicases," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Jaigeeth Deveryshetty & Rahul Chadda & Jenna R. Mattice & Simrithaa Karunakaran & Michael J. Rau & Katherine Basore & Nilisha Pokhrel & Noah Englander & James A. J. Fitzpatrick & Brian Bothner & Edwin, 2023. "Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. Sahiti Kuppa & Jaigeeth Deveryshetty & Rahul Chadda & Jenna R. Mattice & Nilisha Pokhrel & Vikas Kaushik & Angela Patterson & Nalini Dhingra & Sushil Pangeni & Marisa K. Sadauskas & Sajad Shiekh & Ham, 2022. "Rtt105 regulates RPA function by configurationally stapling the flexible domains," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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