This Article Full Text (PDF) Other Versions of this Article: MCB.01118-06v1 26/23/8892    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Guo, C. Articles by Friedberg, E. C. Search for Related Content PubMed PubMed Citation Articles by Guo, C. Articles by Friedberg, E. C.

 Previous Article  |  Next Article 

Mol. Cell. Biol. doi:10.1128/MCB.01118-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Ubiquitin-Binding Motifs in REV1 Protein Are Required For Its Role in the Tolerance of DNA Damage

Laboratory of Molecular Pathology, Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9072, USA; Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Institute for Biochemistry II, Goethe University Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany; Cancer Research UK, Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom; Department of Radiation Genetics, Kyoto University Graduate School of Medicine, Kyoto 606-8501, Japan

^* To whom correspondence should be addressed. Email: friedberg.errol{at}pathology.swmed.edu.

	Abstract

REV1 protein is a eukaryotic member of the Y-family of DNA polymerases involved in the tolerance of DNA damage by replicative bypass. The precise role(s) of REV1 in this process is not known. Here we report that mouse REV1 can physically interact with ubiquitin by using yeast two-hybrid assay and GST pull down. The association of REV1 with ubiquitin requires the ubiquitin-binding motifs (UBMs) located at the C-terminus of REV1. The UBMs also mediates the enhanced association between monoubiquitylated PCNA and REV1. In cells exposed to UV radiation the association of REV1 with replication foci is dependent on functional UBMs. The UBMs of REV1 are shown to contribute to DNA damage tolerance and damage-induced mutagenesis in vivo.

This article has been cited by other articles:

• Choi, J.-Y., Guengerich, F. P. (2008). Kinetic Analysis of Translesion Synthesis Opposite Bulky N2- and O6-Alkylguanine DNA Adducts by Human DNA Polymerase REV1. J. Biol. Chem. 283: 23645-23655 [Abstract] [Full Text]  
• Guo, C., Tang, T.-S., Bienko, M., Dikic, I., Friedberg, E. C. (2008). Requirements for the Interaction of Mouse Pol{kappa} with Ubiquitin and Its Biological Significance. J. Biol. Chem. 283: 4658-4664 [Abstract] [Full Text]  
• Takahashi, S., Sakamoto, A. N., Tanaka, A., Shimizu, K. (2007). AtREV1, a Y-Family DNA Polymerase in Arabidopsis, Has Deoxynucleotidyl Transferase Activity in Vitro. Plant Physiol. 145: 1052-1060 [Abstract] [Full Text]  
• Yang, W., Woodgate, R. (2007). What a difference a decade makes: Insights into translesion DNA synthesis. Proc. Natl. Acad. Sci. USA 104: 15591-15598 [Abstract] [Full Text]  
• Langerak, P., Nygren, A. O.H., Krijger, P. H.L., van den Berk, P. C.M., Jacobs, H. (2007). A/T mutagenesis in hypermutated immunoglobulin genes strongly depends on PCNAK164 modification. J. Exp. Med. 204: 1989-1998 [Abstract] [Full Text]  
• Wood, A., Garg, P., Burgers, P. M. J. (2007). A Ubiquitin-binding Motif in the Translesion DNA Polymerase Rev1 Mediates Its Essential Functional Interaction with Ubiquitinated Proliferating Cell Nuclear Antigen in Response to DNA Damage. J. Biol. Chem. 282: 20256-20263 [Abstract] [Full Text]  
• Parker, J. L., Bielen, A. B., Dikic, I., Ulrich, H. D. (2007). Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase {eta} in Saccharomyces cerevisiae. Nucleic Acids Res 35: 881-889 [Abstract] [Full Text]  
• Crosetto, N., Bienko, M., Dikic, I. (2006). Ubiquitin Hubs in Oncogenic Networks. Mol Cancer Res 4: 899-904 [Abstract] [Full Text]