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Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha.

In an attempt to isolate cofactors capable of influencing estrogen receptor alpha (ERalpha) transcriptional activity, we used yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ERalpha-binding protein. PRMT2 interacted directly with three ERalpha regions including AF-1, DNA binding domain, and hormone binding domain in a ligand-independent fashion. The ERalpha-interacting region on PRMT2 has been mapped to a region encompassing amino acids 133-275. PRMT2 also binds to ERbeta, PR, TRbeta, RARalpha, PPARgamma, and RXRalpha in a ligand-independent manner. PRMT2 enhanced both ERalpha AF-1 and AF-2 transcriptional activity, and the potential methyltransferase activity of PRMT2 appeared pivotal for its coactivator function. In addition, PRMT2 enhanced PR, PPARgamma, and RARalpha-mediated transactivation. Although PRMT2 was found to interact with two other coactivators, the steroid receptor coactivator-1 (SRC-1) and the peroxisome proliferator-activated receptor-interacting protein (PRIP), no synergistic enhancement of ERalpha transcriptional activity was observed when PRMT2 was coexpressed with either PRIP or SRC-1. In this respect PRMT2 differs from coactivators PRMT1 and CARM1 (coactivator-associated arginine methyltransferase). These results suggest that PRMT2 is a novel ERalpha coactivator.

Pubmed ID: 12039952


  • Qi C
  • Chang J
  • Zhu Y
  • Yeldandi AV
  • Rao SM
  • Zhu YJ


The Journal of biological chemistry

Publication Data

August 9, 2002

Associated Grants

  • Agency: NCI NIH HHS, Id: CA 84472
  • Agency: NCI NIH HHS, Id: CA 88898
  • Agency: NIEHS NIH HHS, Id: K08 ES 00356

Mesh Terms

  • Animals
  • COS Cells
  • Cells, Cultured
  • DNA
  • DNA, Complementary
  • Dimerization
  • Estrogen Receptor alpha
  • Gene Library
  • Glutathione Transferase
  • Humans
  • Plasmids
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Arginine N-Methyltransferases
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Estrogen
  • Receptors, Retinoic Acid
  • Transcription Factors
  • Transcription, Genetic
  • Transcriptional Activation
  • Transfection
  • Two-Hybrid System Techniques
  • beta-Galactosidase