Nucleic Acids Research Advance Access originally published online on January 23, 2007
Nucleic Acids Research 2007 35(3):881-889; doi:10.1093/nar/gkl1102
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Nucleic Acids Research, 2007, Vol. 35, No. 3 881-889
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase 
in Saccharomyces cerevisiae
1Cancer Research UK, London Research Institute, Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom 2Max Planck Insitute for Terrestrial Microbiology, Karl-von-Frisch-Straße, D-35043 Marburg, Germany 3Goethe University Medical School, Theodor-Stern-Kai 7, D-60590 Frankfurt, Germany
*To whom the correspondence should be addressed. Tel: +44 1707 625821; Fax: +44 1707 625550; E-mail: helle.ulrich{at}cancer.org.uk
Received June 24, 2006. Revised November 27, 2006. Accepted December 4, 2006.
Bypassing of DNA lesions by damage-tolerant DNA polymerases depends on the interaction of these enzymes with the monoubiquitylated form of the replicative clamp protein, PCNA. We have analyzed the contributions of ubiquitin and PCNA binding to damage bypass and damage-induced mutagenesis in Polymerase 
(encoded by RAD30) from the budding yeast Saccharomyces cerevisiae. We report here that a ubiquitin-binding domain provides enhanced affinity for the ubiquitylated form of PCNA and is essential for in vivo function of the polymerase, but only in conjunction with a basal affinity for the unmodified clamp, mediated by a conserved PCNA interaction motif. We show that enhancement of the interaction and function in damage tolerance does not depend on the ubiquitin attachment site within PCNA. Like its mammalian homolog, budding yeast Polymerase itself is ubiquitylated in a manner dependent on its ubiquitin-binding domain.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.
4 Present address: Paediatric Molecular Pathology Team, Institute of Cancer Research, Sutton, United Kingdom
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