2. Academic Validation
  3. PRMT7 as a unique member of the protein arginine methyltransferase family: A review

PRMT7 as a unique member of the protein arginine methyltransferase family: A review

  • Arch Biochem Biophys. 2019 Apr 15:665:36-45. doi: 10.1016/j.abb.2019.02.014.
Kanishk Jain 1,  Steven G Clarke 2
Affiliations

Affiliations

  • 1 Lineberger Comprehensive Cancer Center and Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, School of Medicine, Chapel Hill, NC, 27599, USA.
  • 2 Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, CA, 90095, USA. Electronic address: [email protected].
PMID: 30802433 DOI: 10.1016/j.abb.2019.02.014
Abstract

Protein arginine methyltransferases (PRMTs) are found in a wide variety of eukaryotic organisms and can regulate gene expression, DNA repair, RNA splicing, and stem Cell Biology. In mammalian cells, nine genes encode a family of sequence-related enzymes; six of these PRMTs catalyze the formation of ω-asymmetric dimethyl derivatives, two catalyze ω-symmetric dimethyl derivatives, and only one (PRMT7) solely catalyzes ω-monomethylarginine formation. Purified recombinant PRMT7 displays a number of unique enzymatic properties including a substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues and a temperature optimum well below 37 °C. Evidence has been presented for crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3. Defects in muscle stem cells (satellite cells) and immune cells are found in mouse PRMT7 homozygous knockouts, while humans lacking PRMT7 are characterized by significant intellectual developmental delays, hypotonia, and facial dysmorphisms. The overexpression of the PRMT7 gene has been correlated with Cancer metastasis in humans. Current research challenges include identifying cellular factors that control PRMT7 expression and activity, identifying the physiological substrates of PRMT7, and determining the effect of methylation on these substrates.

Keywords

Cancer; Epigenetics; Monomethylarginine; PRMT7; Pluripotency; Protein arginine methylation.

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