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Caenorhabditis elegans PRMT‑7 and PRMT‑9 Are Evolutionarily Conserved Protein Arginine Methyltransferases with Distinct Substrate Specificities
journal contribution
posted on 2017-04-25, 00:00 authored by Andrea Hadjikyriacou, Steven G. ClarkeCaenorhabditis elegans protein arginine methyltransferases
PRMT-7 and PRMT-9 are two evolutionarily conserved enzymes, with distinct
orthologs in plants, invertebrates, and vertebrates. Biochemical characterization
of these two enzymes reveals that they share much in common with their
mammalian orthologs. C. elegans PRMT-7 produces only
monomethylarginine (MMA) and preferentially methylates R-X-R motifs
in a broad collection of substrates, including human histone peptides
and RG-rich peptides. In addition, the activity of the PRMT-7 enzyme
is dependent on temperature, the presence of metal ions, and the reducing
agent dithiothreitol. C. elegans PRMT-7 has a substrate
specificity and a substrate preference different from those of mammalian
PRMT7, and the available X-ray crystal structures of the PRMT7 orthologs
show differences in active site architecture. C. elegans PRMT-9, on the other hand, produces symmetric dimethylarginine and
MMA on SFTB-2, the conserved C. elegans ortholog
of human RNA splicing factor SF3B2, indicating a possible role in
the regulation of nematode splicing. In contrast to PRMT-7, C. elegans PRMT-9 appears to be biochemically indistinguishable
from its human ortholog.
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Evolutionarily Conserved Protein Arginine Methyltransferaseselegans orthologX-ray crystal structuresBiochemical characterizationagent dithiothreitolfactor SF 3Bmetal ionsmethylates R-X-R motifsPRMT 7 orthologs show differencessite architectureRNAPRMT -9Distinct Substrate Specificities Caenorhabditis elegans protein arginine methyltransferases PRMT -7substrate specificitySFTBsubstrate preferenceRG-rich peptidesMMAPRMT -7 enzymehistone peptideselegans PRMT -9elegans PRMT -7
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