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Methylation of DNA polymerase ß by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen

Nazim El-Andaloussi^*,1, Taras Valovka^*,1, Magali Toueille^*, Paul O. Hassa^*, Peter Gehrig, Marcela Covic^*, Ulrich Hübscher^* and Michael O. Hottiger^*,2

^* Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Zurich, Switzerland; and

Functional Genomics Center Zurich, Zurich, Switzerland

²Correspondence: Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland. Email: hottiger{at}vetbio.unizh.ch

DNA polymerase ß (pol ß) is a key player in DNA base excision repair (BER). Here, we describe the complex formation of pol ß with the protein arginine methyltransferase 1 (PRMT1). PRMT1 specifically methylated pol ß in vitro and in vivo. Arginine 137 was identified in pol ß as an important target for methylation by PRMT1. Neither the polymerase nor the dRP-lyase activities of pol ß were affected by PRMT1 methylation. However, this modification abolished the interaction of pol ß with proliferating cell nuclear antigen (PCNA). Together, our results provide evidence that PRMT1 methylation of pol ß might play a regulatory role in BER by preventing the involvement of pol ß in PCNA-dependent DNA metabolic events.—El-Andaloussi, N., Valovka, T., Toueille, M., Hassa, P. O., Gehrig, P., Covic, M., Hübscher, U., Hottiger, M. O. Methylation of DNA polymerase ß by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen.

Key Words: posttranslational modification • DNA repair • protein interactions

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