PRMT7 as a unique member of the protein arginine methyltransferase family: A review.
作者： Kanishk Jain , Steven G. Clarke
DOI: 10.1016/J.ABB.2019.02.014
关键词:
摘要: Abstract Protein arginine methyltransferases (PRMTs) are found in a wide variety of eukaryotic organisms and can regulate gene expression, DNA repair, RNA splicing, stem cell biology. In mammalian cells, nine genes encode family sequence-related enzymes; six these PRMTs catalyze the formation ω-asymmetric dimethyl derivatives, two ω-symmetric only one (PRMT7) solely catalyzes ω-monomethylarginine formation. Purified recombinant PRMT7 displays number unique enzymatic properties including substrate preference for residues R-X-R motifs with additional flanking basic amino acid temperature optimum well below 37 °C. Evidence has been presented crosstalk between PRMT5, where methylation histone H4 peptide at R17, substrate, may activate PRMT5 R3. Defects muscle cells (satellite cells) immune mouse Prmt7 homozygous knockouts, while humans lacking characterized by significant intellectual developmental delays, hypotonia, facial dysmorphisms. The overexpression correlated cancer metastasis humans. Current research challenges include identifying cellular factors that control expression activity, physiological substrates PRMT7, determining effect on substrates.
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