The USP1/UAF1 complex promotes double-strand break repair through homologous recombination.

ABSTRACT: Protein ubiquitination plays a key role in the regulation of a variety of DNA repair mechanisms. Protein ubiquitination is controlled by the coordinate activity of ubiquitin ligases and deubiquitinating enzymes (DUBs). The deubiquitinating enzyme USP1 regulates DNA repair and the Fanconi anemia pathway through its association with its WD40 binding partner, UAF1, and through its deubiquitination of two critical DNA repair proteins, FANCD2-Ub and PCNA-Ub. To investigate the function of USP1 and UAF1, we generated USP1⁻/⁻, UAF1⁻/⁻/⁻, and USP1⁻/⁻ UAF1⁻/⁻/⁻ chicken DT40 cell clones. These three clones showed similar sensitivities to chemical cross-linking agents, to a topoisomerase poison, camptothecin, and to an inhibitor of poly(ADP-ribose) polymerase (PARP), indicating that the USP1/UAF1 com

SUBMITTER: Murai J 

PROVIDER: S-EPMC3133424 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature