Protein arginine methylation is a prevalent posttranslational modification in eukaryotic cells. It regulates RNA processing, trafficking and nascent pre-RNA metabolism, receptor-mediated signal transduction, and transcriptional activation processes. PRMT6 was originally identified through a genome-wide search for human protein arginine N-methyltransferase (PRMT) family members. This particular enzyme has type I PRMT activity and with regards to substrate specificity, is functionally distinct from two other previously characterized type I enzymes - PRMT1 and PRMT4. PRMT6 catalyzes the sequential transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine. In addition to methylating target substrates, PRMT6 also displays automethylation activity – this is unusual in that it is the first PRMT to do so. It is localized to the nucleus. Iberg’s group employed the PRMT6 antibody in their studies on effector protein binding to the N-terminal tail of histone 3 (H3)1.
Western Blot: PRMT6 Antibody
They found that PRMT6 is responsible for the H3R2 methylation seen and that this event is a negative regulatory event. Another application of the PRMT6 antibody allowed Canadian researchers to demonstrate that PRMT1 methylation is a key posttranslational modification within the DNA damage response pathway in genome maintenance and cell proliferation2. Mitchell et al performed characterization studies with the PRMT6 antibody to dissect the role of PRMT6 in telomere length and stability3. They have interesting data that strongly suggests PRMT6 directly associates with and methylates TRF2 to help maintain and stabilize telomeres. Researchers at the Fox Cancer Center used the PRMT6 antibody to highlight PRMT6’s role as a negative transcriptional regulator of p53 and its downstream signaling4. PRMT6 antibody enabled Obianyo’s group to develop fluorescein-conjugated activity-based probes (ABPs) based on histone 4 (H4) analogues to characterize the physiological roles of PRMTs by collecting both spatial and temporal data5.
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