Investigation of N-Terminal Phospho-Regulation of Uracil DNA Glycosylase Using Protein Semisynthesis.

ABSTRACT: Uracil DNA Glycosylase (UNG2) is the primary enzyme in humans that prevents the stable incorporation of deoxyuridine monophosphate into DNA in the form of U/A basepairs. During S-phase, UNG2 remains associated with the replication fork through its interactions with two proteins, Proliferating Cell Nuclear Antigen (PCNA) and Replication Protein A (RPA), which are critical for DNA replication and repair. In this work, we used protein semisynthesis and fluorescence anisotropy assays to explore the interactions of UNG2 with PCNA and RPA and to determine the effects of two UNG2 phosphorylation sites (Thr⁶ and Tyr⁸) located within its PCNA-interacting motif (PIP-box). In binding assays, we found that phosphorylation of Thr⁶ or Tyr⁸ on UNG2 can impede P

SUBMITTER: Weiser BP 

PROVIDER: S-EPMC5529330 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature