The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner

Daniel G. Anderson, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

237 Scopus citations

Abstract

Double-stranded DNA break repair and homologous recombination in E. coli are initiated by the RecBCD enzyme, which unwinds and simultaneously degrades DNA from a double-stranded DNA end. This process is stimulated by cis-acting DNA elements, known as χ sites. Using both in vitro pairing and nuclease protection assays, we demonstrate that the translocating RecBCD enzyme, which has been activated by χ, coordinates the preferential loading of the homologous pairing protein, RecA, onto the resultant single-stranded DNA downstream of χ. This facilitated loading of RecA protein results in a substantial increase in both the efficiency and rate of in vitro recombination reactions and offers an explanation for stimulation of recombination and repair in vivo by χ.

Original languageEnglish (US)
Pages (from-to)77-86
Number of pages10
JournalCell
Volume90
Issue number1
DOIs
StatePublished - Jul 11 1997

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner'. Together they form a unique fingerprint.

  • Cite this