Role of replication protein a in double holliday junction dissolution mediated by the BLM-Topo IIIα-RMI1-RMI2 protein complex

Xiaoyu Xue, Steven Raynard, Valeria Busygina, Akhilesh K. Singh, Patrick Sung

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

The conserved BTR complex, composed of the Bloom's syndrome helicase (BLM), topoisomerase IIIα, RMI1, and RMI2, regulates homologous recombination in favor of non-crossover formation via the dissolution of the double Holliday Junction (dHJ). Here we show enhancement of the BTR-mediated dHJ dissolution reaction by the heterotrimeric single-stranded DNA binding protein replication protein A (RPA). Our results suggest that RPA acts by sequestering a single-stranded DNA intermediate during dHJ dissolution. We provide evidence that RPA physically interacts with RMI1. The RPA interaction domain in RMI1 has been mapped, and RMI1 mutants impaired for RPA interaction have been generated. Examination of these mutants ascertains the significance of the RMI1-RPA interaction in dHJ dissolution. Our results thus implicate RPA as a cofactor of the BTR complex in dHJ dissolution.

Original languageEnglish (US)
Pages (from-to)14221-14227
Number of pages7
JournalJournal of Biological Chemistry
Volume288
Issue number20
DOIs
StatePublished - May 17 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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