Human RAD52 interactions with replication protein a and the RAD51 presynaptic complex

Chu Jian Ma, Youngho Kwon, Patrick Sung, Eric C. Greene

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Rad52 is a highly conserved protein involved in the repair of DNA damage. Human RAD52 has been shown to mediate singlestranded DNA (ssDNA) and is synthetic lethal with mutations in other key recombination proteins. For this study, we used single-molecule imaging and ssDNA curtains to examine the binding interactions of human RAD52 with replication protein A (RPA)-coated ssDNA, and we monitored the fate of RAD52 during assembly of the presynaptic complex. We show that RAD52 binds tightly to the RPA-ssDNA complex and imparts an inhibitory effect on RPA turnover. We also found that during presynaptic complex assembly, most of the RPA and RAD52 was displaced from the ssDNA, but some RAD52-RPAssDNA complexes persisted as interspersed clusters surrounded by RAD51 filaments. Once assembled, the presence of RAD51 restricted formation of new RAD52-binding events, but additional RAD52 could bind once RAD51 dissociated from the ssDNA. Together, these results provide new insights into the behavior and dynamics of human RAD52 during presynaptic complex assembly and disassembly.

Original languageEnglish (US)
Pages (from-to)11702-11713
Number of pages12
JournalJournal of Biological Chemistry
Issue number28
StatePublished - Jul 14 2017
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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