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

doi:10.1016/j.molcel.2006.05.038

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 journal › Article › peer-review

177 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 language	English (US)
Pages (from-to)	265-271
Number of pages	7
Journal	Molecular cell
Volume	23
Issue number	2
DOIs	https://doi.org/10.1016/j.molcel.2006.05.038
State	Published - Jul 21 2006

Keywords

DNA

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2006.05.038

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title = "REV1 Protein Interacts with PCNA: Significance of the REV1 BRCT Domain In Vitro and In Vivo",

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.",

keywords = "DNA",

author = "Caixia Guo and Eiichiro Sonoda and Tang, {Tie Shan} and Parker, {Joanne L.} and Bielen, {Aleksandra B.} and Shunichi Takeda and Ulrich, {Helle D.} and Friedberg, {Errol C.}",

note = "Funding Information: We are grateful to Dr. Alan R. Lehmann for MRC5 cells, Dr. J.G. Jansen and Dr. Y. Masuda for REV1 antibodies, Dr. Y. Masuda for purified REV1 protein, Dr. Ivan Dikic for the PCNA-Ub construct and helpful discussion, and Julia Sch{\"o}ning for technical assistance. We thank members of our laboratories for critically reading the manuscript. This study was funded by grant ES11344 from the United States Public Health Service (E.C.F.) and by Cancer Research UK and the German Ministry for Education and Research (H.D.U.). ",

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doi = "10.1016/j.molcel.2006.05.038",

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T2 - Significance of the REV1 BRCT Domain In Vitro and In Vivo

AU - Guo, Caixia

AU - Sonoda, Eiichiro

AU - Tang, Tie Shan

AU - Parker, Joanne L.

AU - Bielen, Aleksandra B.

AU - Takeda, Shunichi

AU - Ulrich, Helle D.

AU - Friedberg, Errol C.

N1 - Funding Information: We are grateful to Dr. Alan R. Lehmann for MRC5 cells, Dr. J.G. Jansen and Dr. Y. Masuda for REV1 antibodies, Dr. Y. Masuda for purified REV1 protein, Dr. Ivan Dikic for the PCNA-Ub construct and helpful discussion, and Julia Schöning for technical assistance. We thank members of our laboratories for critically reading the manuscript. This study was funded by grant ES11344 from the United States Public Health Service (E.C.F.) and by Cancer Research UK and the German Ministry for Education and Research (H.D.U.).

PY - 2006/7/21

Y1 - 2006/7/21

N2 - 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.

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

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