1. Methylation of DNA polymerase ß by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen
- Author
-
Peter Gehrig, Ulrich Hübscher, Michael O. Hottiger, Paul O. Hassa, Marcela Covic, Taras Valovka, Nazim El-Andaloussi, and Magali Toueille
- Subjects
Protein-Arginine N-Methyltransferases ,DNA polymerase ,DNA repair ,viruses ,DNA polymerase II ,Molecular Sequence Data ,DNA polymerase beta ,Methylation ,Biochemistry ,DNA polymerase delta ,Cell Line ,chemistry.chemical_compound ,Proliferating Cell Nuclear Antigen ,Genetics ,Humans ,Immunoprecipitation ,Amino Acid Sequence ,Molecular Biology ,DNA Polymerase beta ,DNA Primers ,Base Sequence ,biology ,Molecular biology ,Recombinant Proteins ,Proliferating cell nuclear antigen ,Repressor Proteins ,chemistry ,biology.protein ,DNA polymerase mu ,Protein Binding ,Biotechnology - Abstract
DNA polymerase beta (pol beta) is a key player in DNA base excision repair (BER). Here, we describe the complex formation of pol beta with the protein arginine methyltransferase 1 (PRMT1). PRMT1 specifically methylated pol beta in vitro and in vivo. Arginine 137 was identified in pol beta as an important target for methylation by PRMT1. Neither the polymerase nor the dRP-lyase activities of pol beta were affected by PRMT1 methylation. However, this modification abolished the interaction of pol beta with proliferating cell nuclear antigen (PCNA). Together, our results provide evidence that PRMT1 methylation of pol beta might play a regulatory role in BER by preventing the involvement of pol beta in PCNA-dependent DNA metabolic events.
- Published
- 2006
- Full Text
- View/download PDF