Drosophila MUS312 interacts with the nucleotide excision repair endonuclease MEI-9 to generate meiotic crossovers.
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.
Yildiz
Ozlem
O
Department of Biology, University of North Carolina - Chapel Hill, Chapel Hill, NC 27599, USA.
Majumder
Samarpan
S
Kramer
Benjamin
B
Sekelsky
Jeff J
JJ
D000818:Animals; D003434:Crossing Over, Genetic; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000235:genetics; D004330:Drosophila / Q000235:genetics* / Q000528:radiation effects; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D019476:Insect Proteins / Q000235:genetics*; D008540:Meiosis; D009687:Nuclear Proteins; D014466:Ultraviolet Rays
D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D019476:Insect Proteins; C097527:MEI-9 protein, Drosophila; C471965:MUS312 protein, Drosophila; D009687:Nuclear Proteins; C095888:xeroderma pigmentosum group F protein