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Arginine methylation regulates DNA polymerase beta

El-Andaloussi, Nazim and Valovka, Taras and Toueille, Magali and Steinacher, Roland and Focke, Frauke and Gehrig, Peter and Covic, Marcela and Hassa, Paul O. and Schär, Primo and Hübscher, Ulrich and Hottiger, Michael O.. (2006) Arginine methylation regulates DNA polymerase beta. Molecular cell, Vol. 22, H. 1. pp. 51-62.

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Official URL: http://edoc.unibas.ch/dok/A5253998

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Abstract

Alterations in DNA repair lead to genomic instability and higher risk of cancer. DNA base excision repair (BER) corrects damaged bases, apurinic sites, and single-strand DNA breaks. Here, a regulatory mechanism for DNA polymerase beta (Pol beta) is described. Pol beta was found to form a complex with the protein arginine methyltransferase 6 (PRMT6) and was specifically methylated in vitro and in vivo. Methylation of Pol beta by PRMT6 strongly stimulated DNA polymerase activity by enhancing DNA binding and processivity, while single nucleotide insertion and dRP-lyase activity were not affected. Two residues, R83 and R152, were identified in Pol beta as the sites of methylation by PRMT6. Genetic complementation of Pol beta knockout cells with R83/152K mutant revealed the importance of these residues for the cellular resistance to DNA alkylating agent. Based on our findings, we propose that PRMT6 plays a role as a regulator of BER.
Faculties and Departments:03 Faculty of Medicine > Departement Biomedizin > Division of Biochemistry and Genetics > Molecular Genetics (Schär)
UniBasel Contributors:Focke, Frauke and Steinacher, Roland and Schär, Primo Leo
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Cell Press
ISSN:1097-2765
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:22 Mar 2012 14:24
Deposited On:22 Mar 2012 13:38

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