Molecular Life Sciences

2018 Edition
| Editors: Robert D. Wells, Judith S. Bond, Judith Klinman, Bettie Sue Siler Masters

Rad51 and Dmc1 Recombinases

Reference work entry



In eukaryotes, Rad51 and its meiosis-specific homologue Dmc1 (disrupted meiotic cDNA1) are key proteins of the homologous recombination (HR) pathway, which is responsible for the error-free repair of DNA double-strand breaks and faithful chromosome segregation. Rad51 and Dmc1 belong to the ubiquitous RecA protein family that is evolutionarily conserved from bacteria to humans. In vitro, Rad51 and Dmc1 show similar biochemical properties. Both proteins can bind ssDNA forming contiguous helical nucleoprotein filaments. The filaments promote the search for homologous dsDNA and DNA strand exchange between identical or nearly identical ssDNA and dsDNA strands, the basic step of homologous recombination. In addition, Rad51 and Dmc1 can promote branch migration of Holliday junctions through a distinct mechanism, which involves protein polymerization and dissociation on DNA. Both proteins bind...

This is a preview of subscription content, log in to check access.


  1. Bugreev DV, Mazin AV (2004) Ca2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity. Proc Natl Acad Sci U S A 101:9988–9993PubMedPubMedCentralCrossRefGoogle Scholar
  2. Bugreev DV, Pezza RJ, Mazina OM, Voloshin ON, Camerini-Otero RD, Mazin AV (2011) The resistance of DMC1 D-loops to dissociation may account for the DMC1 requirement in meiosis. Nat Struct Mol Biol 18:56–60PubMedCrossRefGoogle Scholar
  3. Carreira A, Hilario J, Amitani I, Baskin RJ, Shivji MK, Venkitaraman AR, Kowalczykowski SC (2009) The BRC repeats of BRCA2 modulate the DNA-binding selectivity of RAD51. Cell 136:1032–1043PubMedPubMedCentralCrossRefGoogle Scholar
  4. Kowalczykowski SC (2008) Structural biology: snapshots of DNA repair. Nature 453:463–466PubMedCrossRefGoogle Scholar
  5. Krogh BO, Symington LS (2004) Recombination proteins in yeast. Annu Rev Genet 38:233–271PubMedCrossRefGoogle Scholar
  6. Lim DS, Hasty P (1996) A mutation in mouse rad51 results in an early embryonic lethal that is suppressed by a mutation in p53. Mol Cell Biol 16:7133–7143PubMedPubMedCentralCrossRefGoogle Scholar
  7. Mazin AV, Kowalczykowski SC (1998) The function of the secondary DNA-binding site of RecA protein during DNA strand exchange. EMBO J 17:1161–1168PubMedPubMedCentralCrossRefGoogle Scholar
  8. Murayama Y, Kurokawa Y, Mayanagi K, Iwasaki H (2008) Formation and branch migration of Holliday junctions mediated by eukaryotic recombinases. Nature 451:1018–1021PubMedCrossRefGoogle Scholar
  9. Rossi MJ, Mazina OM, Bugreev DV, Mazin AV (2011) The RecA/RAD51 protein drives migration of Holliday junctions via polymerization on DNA. Proc Natl Acad Sci U S A 108:6432–6437PubMedPubMedCentralCrossRefGoogle Scholar
  10. Sung P (1994) Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science 265:1241–1243PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2018

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyDrexel University College of MedicinePhiladelphiaUSA