Processing of recombination intermediates by the RuvABC proteins

Annu Rev Genet. 1997;31:213-44. doi: 10.1146/annurev.genet.31.1.213.

Abstract

The RuvA, RuvB, and RuvC proteins in Escherichia coli play important roles in the late stages of homologous genetic recombination and the recombinational repair of damaged DNA. Two proteins, RuvA and RuvB, form a complex that promotes ATP-dependent branch migration of Holliday junctions, a process that is important for the formation of heteroduplex DNA. Individual roles for each protein have been defined, with RuvA acting as a specificity factor that targets RuvB, the branch migration motor to the junction. Structural studies indicate that two RuvA tetramers sandwich the junction and hold it in an unfolded square-planar configuration. Hexameric rings of RuvB face each other across the junction and promote a novel dual helicase action that "pumps" DNA through the RuvAB complex, using the free energy provided by ATP hydrolysis. The third protein, RuvC endonuclease, resolves the Holliday junction by introducing nicks into two DNA strands. Genetic and biochemical studies indicate that branch migration and resolution are coupled by direct interactions between the three proteins, possibly by the formation of a RuvABC complex.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / physiology*
  • DNA Helicases*
  • DNA, Bacterial / metabolism
  • DNA-Binding Proteins / physiology*
  • Endodeoxyribonucleases / physiology*
  • Escherichia coli / genetics*
  • Escherichia coli / physiology
  • Escherichia coli Proteins*
  • Humans
  • Recombination, Genetic*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • RuvB protein, Bacteria
  • ruvC protein, E coli
  • Endodeoxyribonucleases
  • Holliday junction DNA helicase, E coli
  • DNA Helicases