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Quantitative genomic analysis of RecA protein binding during DNA double-strand break repair reveals RecBCD action in vivo

  • Charlotte A. Cockram
  • , Milana Filatenkova
  • , Vincent Danos
  • , Meriem El Karoui
  • , David R.F. Leach
  • Institute of Cell Biology
  • University of Edinburgh
  • School of Informatics
  • SynthSys

Research output: Contribution to journal › Article › peer-review

34 Citations (Scopus)

Abstract

Understanding molecular mechanisms in the context of living cells requires the development of new methods of in vivo biochemical analysis to complement established in vitro biochemistry. A critically important molecular mechanism is genetic recombination, required for the beneficial reassortment of genetic information and for DNA double-strand break repair (DSBR). Central to recombination is the RecA (Rad51) protein that assembles into a spiral filament on DNA and mediates genetic exchange. Here we have developed a method that combines chromatin immunoprecipitation with next-generation sequencing (ChIP-Seq) and mathematical modeling to quantify RecA protein binding during the active repair of a single DSB in the chromosome of Escherichia coli. We have used quantitative genomic analysis to infer the key in vivo molecular parameters governing RecA loading by the helicase/ nuclease RecBCD at recombination hot-spots, known as Chi. Our genomic analysis has also revealed that DSBR at the lacZ locus causes a second RecBCD-mediated DSBR event to occur in the terminus region of the chromosome, over 1 Mb away.

Original languageEnglish
Pages (from-to)E4735-E4742
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number34
DOIs
Publication statusPublished - 25 Aug 2015
Externally publishedYes

Keywords

  • DNA repair
  • Homologous recombination
  • Mechanistic modelling
  • RecA
  • RecBCD

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