The PCNA unloader Elg1 promotes recombination at collapsed replication forks in fission yeast.
Ontology highlight
ABSTRACT: Protein-DNA complexes can impede DNA replication and cause replication fork collapse. Whilst it is known that homologous recombination is deployed in such instances to restart replication, it is unclear how a stalled fork transitions into a collapsed fork at which recombination proteins can load. Previously we established assays in Schizosaccharomyces pombe for studying recombination induced by replication fork collapse at the site-specific protein-DNA barrier RTS1 (Nguyen et al., 2015). Here, we provide evidence that efficient recruitment/retention of two key recombination proteins (Rad51 and Rad52) to RTS1 depends on unloading of the polymerase sliding clamp PCNA from DNA by Elg1. We also show that, in the absence of Elg1, reduced recombination is partially suppresse
SUBMITTER: Tamang S
PROVIDER: S-EPMC6544435 | biostudies-literature | 2019 May
REPOSITORIES: biostudies-literature
ACCESS DATA