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The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity.

Protein arginine methylation is a prevalent posttranslational modification in eukaryotic cells that has been implicated in signal transduction, the metabolism of nascent pre-RNA, and the transcriptional activation processes. In searching the human genome for protein arginine N-methyltransferase (PRMT) family members, a novel gene has been found on chromosome 1 that encodes for an apparent methyltransferase, PRMT6. The polypeptide chain of PRMT6 is 41.9 kDa consisting of a catalytic core sequence common to other PRMT enzymes. Expressed as a glutathione S-transferase fusion protein, PRMT6 demonstrates type I PRMT activity, capable of forming both omega-N(G)-monomethylarginine and asymmetric omega-N(G),N(G)-dimethylarginine derivatives on the recombinant glycine- and arginine-rich substrate in a processive manner with a specific activity of 144 pmol methyl groups transferred min(-1) mg(-1) enzyme. A comparison of substrate specificity reveals that PRMT6 is functionally distinct from two previously characterized type I enzymes, PRMT1 and PRMT4. In addition, PRMT6 displays automethylation activity; it is the first PRMT to do so. This novel human PRMT, which resides solely in the nucleus when fused to the green fluorescent protein, joins a family of enzymes with diverse functions within cells.

Pubmed ID: 11724789

Authors

  • Frankel A
  • Yadav N
  • Lee J
  • Branscombe TL
  • Clarke S
  • Bedford MT

Journal

The Journal of biological chemistry

Publication Data

February 1, 2002

Associated Grants

  • Agency: NIEHS NIH HHS, Id: ES07784
  • Agency: NIGMS NIH HHS, Id: GM26020
  • Agency: NIGMS NIH HHS, Id: T32 GM07185

Mesh Terms

  • Amino Acid Sequence
  • Blotting, Northern
  • Catalytic Domain
  • Cell Nucleus
  • Chromosome Mapping
  • Chromosomes, Human, Pair 1
  • Genome, Human
  • Glutathione Transferase
  • Humans
  • Isoenzymes
  • Kinetics
  • Molecular Sequence Data
  • Nuclear Proteins
  • Organ Specificity
  • Protein Processing, Post-Translational
  • Protein-Arginine N-Methyltransferases
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Transcriptional Activation