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The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase.

The TIS21 immediate-early gene and leukemia-associated BTG1 gene encode proteins with similar sequences. Two-hybrid analysis identified a protein that interacts with TIS21 and BTG1. Sequence motifs associated with S-adenosyl-L-methionine binding suggested this protein might have methyltransferase activity. A glutathione S-transferase (GST) fusion of the putative methyltransferase modifies arginine residues, in appropriate protein substrates, to form NG-monomethyl and NG,NG-dimethylarginine (asymmetric). We term the protein- arginine N-methyltransferase (EC gene "PRMT1, " for protein-arginine methyltransferase 1. GST-TIS21 and GST-BTG1 fusion proteins qualitatively and quantitatively modulate endogenous PRMT1 activity, using control and hypomethylated RAT1 cell extracts as methyl-accepting substrates. PRMT1 message appears ubiquitous, and is constitutive in mitogen-stimulated cells. Modulation of PRMT1 activity by transiently expressed regulatory subunits may be an additional mode of signal transduction following ligand stimulation.

Pubmed ID: 8663146


  • Lin WJ
  • Gary JD
  • Yang MC
  • Clarke S
  • Herschman HR


The Journal of biological chemistry

Publication Data

June 21, 1996

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM24797
  • Agency: NIGMS NIH HHS, Id: GM26020

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA Primers
  • DNA, Complementary
  • Escherichia coli
  • Genes, Tumor Suppressor
  • Glutathione Transferase
  • Humans
  • Immediate-Early Proteins
  • Intracellular Signaling Peptides and Proteins
  • Leukemia, Lymphocytic, Chronic, B-Cell
  • Macromolecular Substances
  • Mammals
  • Methyltransferases
  • Molecular Sequence Data
  • Neoplasm Proteins
  • Open Reading Frames
  • Polymerase Chain Reaction
  • Protein Biosynthesis
  • Protein Structure, Secondary
  • Protein-Arginine N-Methyltransferases
  • Proteins
  • Rats
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid
  • Tumor Suppressor Proteins