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

FASEB J. 2007 Jan;21(1):26-34. doi: 10.1096/fj.06-6194com. Epub 2006 Nov 20.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cell Line
  • DNA Polymerase beta / chemistry
  • DNA Polymerase beta / metabolism*
  • DNA Primers
  • Humans
  • Immunoprecipitation
  • Methylation
  • Molecular Sequence Data
  • Proliferating Cell Nuclear Antigen / metabolism*
  • Protein Binding
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Repressor Proteins / metabolism*


  • DNA Primers
  • Proliferating Cell Nuclear Antigen
  • Recombinant Proteins
  • Repressor Proteins
  • PRMT1 protein, human
  • Protein-Arginine N-Methyltransferases
  • DNA Polymerase beta