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Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain.

The Journal of biological chemistry (2007-10-11)
Joyce Sayegh, Kristofor Webb, Donghang Cheng, Mark T Bedford, Steven G Clarke
ABSTRACT

Human protein arginine methyltransferase PRMT8 has been recently described as a type I enzyme in brain that is localized to the plasma membrane by N-terminal myristoylation. The amino acid sequence of human PRMT8 is almost 80% identical to human PRMT1, the major protein arginine methyltransferase activity in mammalian cells. However, the activity of a recombinant PRMT8 GST fusion protein toward methyl-accepting substrates is much lower than that of a GST fusion of PRMT1. We show here that both His-tagged and GST fusion species lacking the initial 60 amino acid residues of PRMT8 have enhanced enzymatic activity, suggesting that the N-terminal domain may regulate PRMT8 activity. This conclusion is supported by limited proteolysis experiments showing an increase in the activity of the digested full-length protein, consistent with the loss of the N-terminal domain. In contrast, the activity of the N-terminal truncated protein was slightly diminished by limited proteolysis. Significantly, we detect automethylation at two sites in the N-terminal domain, as well as binding sites for SH3 domain-containing proteins. We suggest that the N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
PRMT8 human, recombinant, expressed in baculovirus infected Sf9 cells, ≥90% (SDS-PAGE)
Sigma-Aldrich
Anti-PRMT2 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

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