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METTL21A

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https://www.readbyqxmd.com/read/26115316/saccharomyces-cerevisiae-eukaryotic-elongation-factor-1a-eef1a-is-methylated-at-lys-390-by-a-mettl21-like-methyltransferase
#1
Magnus E Jakobsson, Erna Davydova, Jędrzej Małecki, Anders Moen, Pål Ø Falnes
The human methyltransferases (MTases) METTL21A and VCP-KMT (METTL21D) were recently shown to methylate single lysine residues in Hsp70 proteins and in VCP, respectively. The yet uncharacterized MTase encoded by the YNL024C gene in Saccharomyces cerevisiae shows high sequence similarity to METTL21A and VCP-KMT, as well as to their uncharacterized paralogues METTL21B and METTL21C. Despite being most similar to METTL21A, the Ynl024c protein does not methylate yeast Hsp70 proteins, which were found to be unmethylated on the relevant lysine residue...
2015: PloS One
https://www.readbyqxmd.com/read/25144183/selenium-based-s-adenosylmethionine-analog-reveals-the-mammalian-seven-beta-strand-methyltransferase-mettl10-to-be-an-ef1a1-lysine-methyltransferase
#2
Tadahiro Shimazu, Joaquin Barjau, Yoshihiro Sohtome, Mikiko Sodeoka, Yoichi Shinkai
Lysine methylation has been extensively studied in histones, where it has been shown to provide specific epigenetic marks for the regulation of gene expression; however, the molecular mechanism and physiological function of lysine methylation in proteins other than histones remains to be fully addressed. To better understand the substrate diversity of lysine methylation, S-adenosylmethionine (SAM) derivatives with alkyne-moieties have been synthesized. A selenium-based SAM analog, propargylic Se-adenosyl-l-selenomethionine (ProSeAM), has a wide spectrum of reactivity against various lysine methyltransferases (KMTs) with sufficient stability to support enzymatic reactions in vitro...
2014: PloS One
https://www.readbyqxmd.com/read/23921388/identification-and-characterization-of-a-novel-human-methyltransferase-modulating-hsp70-protein-function-through-lysine-methylation
#3
Magnus E Jakobsson, Anders Moen, Luc Bousset, Wolfgang Egge-Jacobsen, Stefan Kernstock, Ronald Melki, Pål Ø Falnes
Hsp70 proteins constitute an evolutionarily conserved protein family of ATP-dependent molecular chaperones involved in a wide range of biological processes. Mammalian Hsp70 proteins are subject to various post-translational modifications, including methylation, but for most of these, a functional role has not been attributed. In this study, we identified the methyltransferase METTL21A as the enzyme responsible for trimethylation of a conserved lysine residue found in several human Hsp70 (HSPA) proteins. This enzyme, denoted by us as HSPA lysine (K) methyltransferase (HSPA-KMT), was found to catalyze trimethylation of various Hsp70 family members both in vitro and in vivo, and the reaction was stimulated by ATP...
September 27, 2013: Journal of Biological Chemistry
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