REV1 Protein Interacts with PCNA: Significance of the REV1 BRCT Domain In Vitro and In Vivo

Caixia Guo, Eiichiro Sonoda, Tie Shan Tang, Joanne L. Parker, Aleksandra B. Bielen, Shunichi Takeda, Helle D. Ulrich, Errol C. Friedberg

Research output: Contribution to journalArticle

144 Scopus citations

Abstract

REV1 protein, a eukaryotic member of the Y family of DNA polymerases, is involved in the tolerance of DNA damage by translesion DNA synthesis. It is unclear how REV1 is recruited to replication foci in cells. Here, we report that mouse REV1 can bind directly to PCNA and that monoubiquitylation of PCNA enhances this interaction. The interaction between REV1 protein and PCNA requires a functional BRCT domain located near the N terminus of the former protein. Deletion or mutational inactivation of the BRCT domain abolishes the targeting of REV1 to replication foci in unirradiated cells, but not in UV-irradiated cells. In vivo studies in both chicken DT40 cells and yeast directly support the requirement of the BRCT domain of REV1 for cell survival and DNA damage-induced mutagenesis.

Original languageEnglish (US)
Pages (from-to)265-271
Number of pages7
JournalMolecular cell
Volume23
Issue number2
DOIs
StatePublished - Jul 21 2006

Keywords

  • DNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Guo, C., Sonoda, E., Tang, T. S., Parker, J. L., Bielen, A. B., Takeda, S., Ulrich, H. D., & Friedberg, E. C. (2006). REV1 Protein Interacts with PCNA: Significance of the REV1 BRCT Domain In Vitro and In Vivo. Molecular cell, 23(2), 265-271. https://doi.org/10.1016/j.molcel.2006.05.038