The fission yeast BLM homolog Rqh1 promotes meiotic recombination.

Publication Type:

Journal Article

Source:

Genetics, Volume 179, Issue 3, p.1157-67 (2008)

Keywords:

2008, Alleles, Basic Sciences Division, Center-Authored Paper, Crossing Over, Genetic, DNA Breaks, Double-Stranded, DNA Helicases, DNA repair, GENE CONVERSION, Gene Duplication, Genomics Core Facility, MEIOSIS, Mutation, Protein Structure, Tertiary, Recombination, Genetic, RecQ Helicases, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Homology, Amino Acid, Shared Resources, Spores, Fungal

Abstract:

RecQ helicases are found in organisms as diverse as bacteria, fungi, and mammals. These proteins promote genome stability, and mutations affecting human RecQ proteins underlie premature aging and cancer predisposition syndromes, including Bloom syndrome, caused by mutations affecting the BLM protein. In this study we show that mutants lacking the Rqh1 protein of the fission yeast Schizosaccharomyces pombe, a RecQ and BLM homolog, have substantially reduced meiotic recombination, both gene conversions and crossovers. The relative proportion of gene conversions having associated crossovers is unchanged from that in wild type. In rqh1 mutants, meiotic DNA double-strand breaks are formed and disappear with wild-type frequency and kinetics, and spore viability is only moderately reduced. Genetic analyses and the wild-type frequency of both intersister and interhomolog joint molecules argue against these phenotypes being explained by an increase in intersister recombination at the expense of interhomolog recombination. We suggest that Rqh1 extends hybrid DNA and biases the recombination outcome toward crossing over. Our results contrast dramatically with those from the budding yeast ortholog, Sgs1, which has a meiotic antirecombination function that suppresses recombination events involving more than two DNA duplexes. These observations underscore the multiple recombination functions of RecQ homologs and emphasize that even conserved proteins can be adapted to play different roles in different organisms.