Interaction of branch migration translocases with the holliday junction-resolving enzyme and their implications in holliday junction resolution

Cristina Cañas, Yuki Suzuki, Chiara Marchisone, Begoña Carrasco, Verónica Freire-Benéitez, Kunio Takeyasu, Juan C. Alonso, Silvia Ayora

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Double-strand break repair involves the formation of Holliday junction (HJ) structures that need to be resolved to promote correct replication and chromosomal segregation. The molecular mechanisms of HJ branch migration and/or resolution are poorly characterized in Firmicutes. Genetic evidence suggested that the absence of the RuvAB branch migration translocase and the RecU HJ resolvase is synthetically lethal in Bacillus subtilis, whereas a recU recG mutant was viable. In vitro RecU, which is restricted to bacteria of the Firmicutes phylum, binds HJs with high affinity. In this work we found that RecU does not bind simultaneously with RecG to a HJ. RuvB by interacting with RecU bound to the central region of HJ DNA, loses its nonspecific association with DNA, and re-localizes with RecU to form a ternary complex. RecU cannot stimulate the ATPase or branch migration activity of RuvB. The presence of RuvB·ATPγS greatly stimulates RecU-mediated HJ resolution, but the addition of ATP or RuvA abolishes this stimulatory effect. A RecU·HJ·RuvAB complex might be formed. RecU does not increase the RuvAB activities but slightly inhibits them.

Original languageEnglish
Pages (from-to)17634-17646
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number25
DOIs
Publication statusPublished - 2014 Jun 20

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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