Action of RecBCD enzyme on Holliday structures made by RecA

Berndt Marino Muller, P E Boehmer, P T Emmerson, S C West

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4 Citations (Scopus)

Abstract

In vitro, Escherichia coli RecA protein acts upon gapped and partially homologous linear duplex DNA to generate recombination products linked by Holliday junctions. When strand exchange reactions are supplemented with purified RecBCD enzyme, we observe the formation of products that resemble "patch" recombinants. The formation of "splice" recombinant products was not observed. The individual subunits, RecB, RecC, or RecD, had no effect on RecA protein-mediated strand exchange nor on the Holliday junctions formed in the reaction. Analysis of the way in which patch products arise indicates exonucleolytic digestion of the linear arms of the recombination intermediates (alpha-structures) by RecBCD enzyme. We find no evidence for specific resolution events at the site of the Holliday junction by RecBCD enzyme using these DNA substrates.

Original languageEnglish
Pages (from-to)19028-19033
Number of pages6
JournalThe Journal of Biological Chemistry
Volume266
Issue number28
Publication statusPublished - 5 Oct 1991

Keywords

  • escherichia-coli reca
  • double-stranded DNA
  • endonuclease-VII
  • genetic-recombination
  • cruciform DNA
  • homologous recombination
  • saccharomyces-cerevisiae
  • K-12 reveals
  • RUV region
  • junctions

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