Role of the Human RAD51 Protein in Homologous Recombination and Double-Stranded-Break Repair

Trends Biochem Sci. 1998 Jul;23(7):247-51. doi: 10.1016/s0968-0004(98)01232-8.

Abstract

Eukaryotic cells possess several mechanisms for repairing double-stranded breaks in DNA. One mechanism involves genetic recombination with an intact sister duplex. The recent identification of the RAD51 protein, a eukaryotic homologue of Escherichia coli RecA, represents a landmark discovery in our understanding of the key reactions in this repair pathway. RAD51 is similar to RecA, both biochemically and structurally: it promotes homologous pairing and strand exchange within a regular nucleoprotein filament. The isolation of yeast and human RecA homologues shows that homologous recombination and recombinational repair have been conserved throughout evolution. The goal is now to identify other factors involved in recombinational repair and to define their roles in this essential process.

Publication types

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

MeSH terms

  • Animals
  • DNA Repair
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Evolution, Molecular
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Humans
  • Rad51 Recombinase
  • Rec A Recombinases / genetics
  • Rec A Recombinases / metabolism
  • Recombination, Genetic
  • Replication Protein A
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • RPA1 protein, human
  • Replication Protein A
  • Saccharomyces cerevisiae Proteins
  • RAD51 protein, S cerevisiae
  • RAD51 protein, human
  • Rad51 Recombinase
  • Rec A Recombinases