Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells

Cell. 2001 Jan 26;104(2):259-68. doi: 10.1016/s0092-8674(01)00210-0.

Abstract

During homologous recombination, DNA strand exchange leads to Holliday junction formation. The movement, or branch migration, of this junction along DNA extends the length of the heteroduplex joint. In prokaryotes, branch migration and Holliday junction resolution are catalyzed by the RuvA and RuvB proteins, which form a complex with RuvC resolvase to form a "resolvasome". Mammalian cell-free extracts have now been fractionated to reveal analogous activities. An ATP-dependent branch migration activity, which migrates junctions through >2700 bp, cofractionates with the Holliday junction resolvase during several chromatographic steps. Together, the two activities promote concerted branch migration/resolution reactions similar to those catalyzed by E. coli RuvABC, highlighting the preservation of this essential pathway in recombination and DNA repair from prokaryotes to mammals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Cell Fractionation
  • Cell Line
  • Cell-Free System
  • Cricetinae
  • DNA / metabolism*
  • DNA Helicases*
  • DNA Repair
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases / genetics
  • Endodeoxyribonucleases / metabolism*
  • Escherichia coli / chemistry
  • Escherichia coli Proteins*
  • Holliday Junction Resolvases
  • Humans
  • Macromolecular Substances
  • Nucleic Acid Conformation
  • Rabbits
  • Recombination, Genetic*

Substances

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