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Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase η in Saccharomyces cerevisiae

  • 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 {eta} (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 {eta} itself is ubiquitylated in a manner dependent on its ubiquitin-binding domain.

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Author:Joanne L. Parker, Aleksandra B. Bielen, Ivan ĐikićORCiDGND, Helle D. Ulrich
URN:urn:nbn:de:hebis:30-47175
DOI:https://doi.org/10.1093/nar/gkl1102
ISSN:1362-4962
ISSN:0305-1048
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/PMC1807963
Parent Title (English):Nucleic Acids Research
Publisher:Oxford Univ. Press
Place of publication:Oxford
Document Type:Article
Language:English
Date of Publication (online):2007/01/23
Date of first Publication:2007/01/23
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2007/08/06
Volume:35
Issue:3
Page Number:9
First Page:881
Last Page:889
Note:
© 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.
Source:Nucleic Acids Research 2007, Vol. 35, No. 3, 881-889, doi:10.1093/nar/gkl1102. - http://nar.oxfordjournals.org/cgi/content/abstract/35/3/881
HeBIS-PPN:189553715
Institutes:Medizin / Medizin
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Sammlung Biologie / Sondersammelgebiets-Volltexte
Licence (German):License LogoCreative Commons - Namensnennung-Nicht kommerziell 2.0