Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis

Caixia Guo, Paula L. Fischhaber, Margaret J. Luk-Paszyc, Yuji Masuda, Jing Zhou, Kenji Kamiya, Caroline Kisker, Errol C. Friedberg

Research output: Contribution to journalArticlepeer-review

274 Scopus citations

Abstract

Polκ and Rev1 are members of the Y family of DNA polymerases involved in tolerance to DNA damage by replicative bypass [translesion DNA synthesis (TLS)]. We demonstrate that mouse Rev1 protein physically associates with Polκ. We show too that Rev1 interacts independently with Rev7 (a subunit of a TLS polymerase, Polζ) and with two other Y-family polymerases, Polι and Polη. Mouse Polκ, Rev7, Polι, and Polη each bind to the same ∼100 amino acid C-terminal region of Rev1. Furthermore, Rev7 competes directly with Polκ for binding to the Rev1 C-terminus. Notwithstanding the physical interaction between Rev1 and Polκ, the DNA polymerase activity of each measured by primer extension in vitro is unaffected by the complex, either when extending normal primer-termini, when bypassing a single thymine glycol lesion, or when extending certain mismatched primer termini. Our observations suggest that Rev1 plays a role(s) in mediating protein-protein interactions among DNA polymerases required for TLS. The precise function(s) of these interactions during TLS remains to be determined.

Original languageEnglish (US)
Pages (from-to)6621-6630
Number of pages10
JournalEMBO Journal
Volume22
Issue number24
DOIs
StatePublished - Dec 15 2003

Keywords

  • DNA polymerases
  • Mutagenesis
  • Polκ
  • Rev1
  • Translesion DNA synthesis

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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