Drosophila MUS312 interacts with the nucleotide excision repair endonuclease MEI-9 to generate meiotic crossovers

Mol Cell. 2002 Dec;10(6):1503-9. doi: 10.1016/s1097-2765(02)00782-7.

Abstract

MEI-9 is the Drosophila homolog of the human structure-specific DNA endonuclease XPF. Like XPF, MEI-9 functions in nucleotide excision repair and interstrand crosslink repair. MEI-9 is also required to generate meiotic crossovers, in a function thought to be associated with resolution of Holliday junction intermediates. We report here the identification of MUS312, a protein that physically interacts with MEI-9. We show that mutations in mus312 elicit a meiotic phenotype identical to that of mei-9 mutants. A missense mutation in mei-9 that disrupts the MEI-9-MUS312 interaction abolishes the meiotic function of mei-9 but does not affect the DNA repair functions of mei-9. We propose that MUS312 facilitates resolution of meiotic Holliday junction intermediates by MEI-9.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crossing Over, Genetic
  • DNA Repair*
  • DNA-Binding Proteins / genetics
  • Drosophila / genetics*
  • Drosophila / radiation effects
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Humans
  • Insect Proteins / genetics*
  • Meiosis
  • Nuclear Proteins*
  • Ultraviolet Rays

Substances

  • DNA-Binding Proteins
  • Drosophila Proteins
  • Insect Proteins
  • MEI-9 protein, Drosophila
  • MUS312 protein, Drosophila
  • Nuclear Proteins
  • xeroderma pigmentosum group F protein