Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis

Nat Commun. 2017 Dec 5;8(1):1941. doi: 10.1038/s41467-017-02164-1.

Abstract

DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively. However, whether post-translational modifications of Polη are involved in these processes remains largely unknown. Here, we reported that human Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase upon DNA damage. Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected. Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin. Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology
  • Cell Line, Tumor
  • Cisplatin / pharmacology
  • DNA / biosynthesis*
  • DNA Damage*
  • DNA Repair*
  • DNA Replication
  • DNA-Directed DNA Polymerase / metabolism*
  • HEK293 Cells
  • Humans
  • Mutagenesis
  • N-Acetylglucosaminyltransferases / metabolism*
  • Polyubiquitin
  • Protein Processing, Post-Translational
  • Pyrimidine Dimers
  • Ubiquitination
  • Ultraviolet Rays

Substances

  • Antineoplastic Agents
  • Pyrimidine Dimers
  • Polyubiquitin
  • DNA
  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase
  • DNA-Directed DNA Polymerase
  • Rad30 protein
  • Cisplatin