Structural and functional analyses of the DMC1-M200V polymorphism found in the human population

Nucleic Acids Res. 2008 Jul;36(12):4181-90. doi: 10.1093/nar/gkn362. Epub 2008 Jun 19.

Abstract

The M200V polymorphism of the human DMC1 protein, which is an essential, meiosis-specific DNA recombinase, was found in an infertile patient, raising the question of whether this homozygous human DMC1-M200V polymorphism may cause infertility by affecting the function of the human DMC1 protein. In the present study, we determined the crystal structure of the human DMC1-M200V variant in the octameric-ring form. Biochemical analyses revealed that the human DMC1-M200V variant had reduced stability, and was moderately defective in catalyzing in vitro recombination reactions. The corresponding M194V mutation introduced in the Schizosaccharomyces pombe dmc1 gene caused a significant decrease in the meiotic homologous recombination frequency. Together, these structural, biochemical and genetic results provide extensive evidence that the human DMC1-M200V mutation impairs its function, supporting the previous interpretation that this single-nucleotide polymorphism is a source of human infertility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arginine / chemistry
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / genetics*
  • Cell Cycle Proteins / metabolism
  • Chromosome Pairing
  • Crystallography, X-Ray
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism
  • Humans
  • Meiosis / genetics
  • Molecular Sequence Data
  • Polymorphism, Single Nucleotide*
  • Recombinases / genetics
  • Recombination, Genetic
  • Schizosaccharomyces pombe Proteins / genetics

Substances

  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Dmc1 protein, S pombe
  • Recombinases
  • Schizosaccharomyces pombe Proteins
  • DNA
  • Arginine
  • DMC1 protein, human