The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51

Jean Yves Masson, Adelina A. Davies, Nasser Hajibagheri, Eric Van Dyck, Fiona E. Benson, Alicja Z. Stasiak, Andrzej Stasiak, Stephen C. West*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

118 Citations (Scopus)

Abstract

Eukaryotic cells encode two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, which are required for meiotic recombination. Rad51, like E. coli RecA, forms helical nucleoprotein filaments that promote joint molecule and heteroduplex DNA formation. Electron microscopy reveals that the human meiosis-specific recombinase Dmc1 forms ring structures that bind single-stranded (ss) and double-stranded (ds) DNA. The protein binds preferentially to ssDNA tails and gaps in duplex DNA. hDmc1-ssDNA complexes exhibit an irregular, often compacted structure, and promote strand-transfer reactions with homologous duplex DNA. hDmc1 binds duplex DNA with reduced affinity to form nucleoprotein complexes. In contrast to helical RecA/Rad51 filaments, however, Dmc1 filaments are composed of a linear array of stacked protein rings. Consistent with the requirement for two recombinases in meiotic recombination, hDmc1 interacts directly with hRad51.

Original languageEnglish
Pages (from-to)6552-6560
Number of pages9
JournalEMBO Journal
Volume18
Issue number22
DOIs
Publication statusPublished - 15 Nov 1999
Externally publishedYes

Keywords

  • Meiotic recombination
  • Recombinases
  • Ring structures
  • hDmc1
  • hRad51

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