Motoring along with the bacterial RecA protein

Nat Rev Mol Cell Biol. 2007 Feb;8(2):127-38. doi: 10.1038/nrm2099. Epub 2007 Jan 17.

Abstract

The recombinases of the RecA family are often viewed only as DNA-pairing proteins - they bind to one DNA segment, align it with homologous sequences in another DNA segment, promote an exchange of DNA strands and then dissociate. To a first approximation, this description seems to fit the eukaryotic (Rad51 and Dmc1) and archaeal (RadA) RecA homologues. However, the bacterial RecA protein does much more, coupling ATP hydrolysis with DNA-strand exchange in a manner that greatly expands its repertoire of activities. This article explores the protein activities and experimental results that have identified RecA as a motor protein.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / physiology
  • DNA Replication*
  • DNA, Bacterial / genetics
  • DNA, Bacterial / metabolism
  • Gene Expression Regulation, Bacterial*
  • Gene Expression Regulation, Enzymologic*
  • Hydrolysis
  • Models, Genetic
  • Molecular Motor Proteins / chemistry
  • Molecular Motor Proteins / genetics*
  • Molecular Motor Proteins / physiology
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rec A Recombinases / chemistry
  • Rec A Recombinases / genetics*
  • Rec A Recombinases / physiology
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Molecular Motor Proteins
  • Adenosine Triphosphate
  • Rec A Recombinases