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Nat Struct Mol Biol. 2011 Jan;18(1):56-60. doi: 10.1038/nsmb.1946. Epub 2010 Dec 12.

The resistance of DMC1 D-loops to dissociation may account for the DMC1 requirement in meiosis.

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Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.

Erratum in

  • Nat Struct Mol Biol. 2011 Sep;18(9):1084.
  • Nat Struct Mol Biol. 2013 Feb;20(2):244.


The ubiquitously expressed Rad51 recombinase and the meiosis-specific Dmc1 recombinase promote the formation of strand-invasion products (D-loops) between homologous molecules. Strand-invasion products are processed by either the double-strand break repair (DSBR) or synthesis-dependent strand annealing (SDSA) pathway. D-loops destined to be processed by SDSA need to dissociate, producing non-crossovers, and those destined for DSBR should resist dissociation to generate crossovers. The mechanism that channels recombination intermediates into different homologous-recombination pathways is unknown. Here we show that D-loops in a human DMC1-driven reaction are substantially more resistant to dissociation by branch-migration proteins such as RAD54 than those formed by RAD51. We propose that the intrinsic resistance to dissociation of DMC1 strand-invasion intermediates may account for why DMC1 is essential to ensure the proper segregation of chromosomes in meiosis.

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