C-elegans ring finger protein RNF-113 is involved in interstrand DNA crosslink repair and interacts with a RAD51C homolog

Hyojin Lee, Arno F. Alpi, Mi So Park, Ann Rose, Hyeon-Sook Koo

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    The Fanconi anemia (FA) pathway recognizes interstrand DNA crosslinks (ICLs) and contributes to their conversion into double-strand DNA breaks, which can be repaired by homologous recombination. Seven orthologs of the 15 proteins associated with Fanconi anemia are functionally conserved in the model organism C. elegans. Here we report that RNF-113, a ubiquitin ligase, is required for RAD-51 focus formation after inducing ICLs in C. elegans. However, the formation of foci of RPA-1 or FCD-2/FANCD2 in the FA pathway was not affected by depletion of RNF-113. Nevertheless, the RPA-1 foci formed did not disappear with time in the depleted worms, implying serious defects in ICL repair. As a result, RNF-113 depletion increased embryonic lethality after ICL treatment in wild-type worms, but it did not increase the ICL-induced lethality of rfs-1/rad51C mutants. In addition, the persistence of RPA-1 foci was suppressed in doubly-deficient rnf-113;rfs-1 worms, suggesting that there is an epistatic interaction between the two genes. These results lead us to suggest that RNF-113 and RFS-1 interact to promote the displacement of RPA-1 by RAD-51 on single-stranded DNA derived from ICLs.

    Original languageEnglish
    Article number600701
    Number of pages10
    JournalPLoS ONE
    Volume8
    Issue number3
    DOIs
    Publication statusPublished - 28 Mar 2013

    Keywords

    • CORE COMPLEX
    • STRAND BREAK REPAIR
    • RECOMBINATION
    • CAENORHABDITIS-ELEGANS
    • FANCD2
    • REPLICATION STRESS
    • FANCONI-ANEMIA PATHWAY
    • CANCER
    • SACCHAROMYCES-CEREVISIAE
    • DAMAGE RESPONSE

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