REV1 protein interacts with PCNA: Significance of the REV1 BRCT domain in vitro and in vivo

被引：174

作者：

Guo, Caixia

Sonoda, Eiichiro

Tang, Tie-Shan

Parker, Joanne L.

Bielen, Aleksandra B.

Takeda, Shunichi

Ulrich, Helle D.

Friedberg, Errol C. ^{[1
]}

机构：

[1] Univ Texas, SW Med Ctr, Lab Mol Pathol, Dept Pathol, Dallas, TX 75390 USA

[2] Univ Texas, SW Med Ctr, Dept Physiol, Dallas, TX 75390 USA

[3] Kyoto Univ, Grad Sch Med, Dept Radiat Genet, Kyoto 6068501, Japan

[4] Canc Res UK, Clare Hall Labs, S Mimms EN6 3LD, Herts, England

来源：

MOLECULAR CELL | 2006年 / 23卷 / 02期

关键词：

D O I：

10.1016/j.molcel.2006.05.038

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

收藏

页码：265 / 271

页数：7

相关论文

共 26 条

[1] Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis [J].

Bienko, M ;

Green, CM ;

Crosetto, N ;

Rudolf, F ;

Zapart, G ;

Coull, B ;

Kannouche, P ;

Wider, G ;

Peter, M ;

Lehmann, AR ;

Hofmann, K ;

Dikic, I .

SCIENCE, 2005, 310 (5755) :1821-1824

[2] INCREASED RATIO OF TARGETED TO RANDOM INTEGRATION AFTER TRANSFECTION OF CHICKEN B-CELL LINES [J].

BUERSTEDDE, JM ;

TAKEDA, S .

CELL, 1991, 67 (01) :179-188

[3] Trading places: How do DNA polymerases switch during translesion DNA synthesis? [J].

Friedberg, EC ;

Lehmann, AR ;

Fuchs, RPP .

MOLECULAR CELL, 2005, 18 (05) :499-505

[4] NEW YEAST-ESCHERICHIA-COLI SHUTTLE VECTORS CONSTRUCTED WITH INVITRO MUTAGENIZED YEAST GENES LACKING 6-BASE PAIR RESTRICTION SITES [J].

GIETZ, RD ;

SUGINO, A .

GENE, 1988, 74 (02) :527-534

[5] Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis [J].

Guo, CX ;

Fischhaber, PL ;

Luk-Paszyc, MJ ;

Masuda, Y ;

Zhou, J ;

Kamiya, K ;

Kisker, C ;

Friedberg, EC .

EMBO JOURNAL, 2003, 22 (24) :6621-6630

[6] RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO [J].

Hoege, C ;

Pfander, B ;

Moldovan, GL ;

Pyrowolakis, G ;

Jentsch, S .

NATURE, 2002, 419 (6903) :135-141

[7] The BRCA1 C-terminal domain: structure and function [J].

Huyton, T ;

Bates, PA ;

Zhang, XD ;

Sternberg, MJE ;

Freemont, PS .

MUTATION RESEARCH-DNA REPAIR, 2000, 460 (3-4) :319-332

[8] The BRCT domain of mammalian Rev1 is involved in regulating DNA translesion synthesis [J].

Jansen, JG ;

Tsaalbi-Shtylik, A ;

Langerak, P ;

Calléja, F ;

Meijers, CM ;

Jacobs, H ;

de Wind, N .

NUCLEIC ACIDS RESEARCH, 2005, 33 (01) :356-365

[9] Domain structure, localization, and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells [J].

Kannouche, P ;

Broughton, BC ;

Volker, M ;

Hanaoka, F ;

Mullenders, LHF ;

Lehmann, AR .

GENES & DEVELOPMENT, 2001, 15 (02) :158-172

[10] Interaction of human DNA polymerase η with monoubiquitinated PCNA:: A possible mechanism for the polymerase switch in response to DNA damage [J].

Kannouche, PL ;

Wing, J ;

Lehmann, AR .

MOLECULAR CELL, 2004, 14 (04) :491-500