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HEMK2

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https://www.readbyqxmd.com/read/26797129/substrate-specificity-of-the-hemk2-protein-glutamine-methyltransferase-and-identification-of-novel-substrates
#1
Denis Kusevic, Srikanth Kudithipudi, Albert Jeltsch
Bacterial HEMK2 homologs initially had been proposed to be involved in heme biogenesis or to function as adenine DNA methyltransferase. Later it was shown that this family of enzymes has protein glutamine methyltransferase activity, and they methylate the glutamine residue in the GGQ motif of ribosomal translation termination factors. The murine HEMK2 enzyme methylates Gln(185) of the eukaryotic translation termination factor eRF1. We have employed peptide array libraries to investigate the peptide sequence recognition specificity of murine HEMK2...
March 18, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/18539146/hemk2-protein-encoded-on-human-chromosome-21-methylates-translation-termination-factor-erf1
#2
Sabine Figaro, Nathalie Scrima, Richard H Buckingham, Valérie Heurgué-Hamard
The ubiquitous tripeptide Gly-Gly-Gln in class 1 polypeptide release factors triggers polypeptide release on ribosomes. The Gln residue in both bacterial and yeast release factors is N5-methylated, despite their distinct evolutionary origin. Methylation of eRF1 in yeast is performed by the heterodimeric methyltransferase (MTase) Mtq2p/Trm112p, and requires eRF3 and GTP. Homologues of yeast Mtq2p and Trm112p are found in man, annotated as an N6-DNA-methyltransferase and of unknown function. Here we show that the human proteins methylate human and yeast eRF1...
July 9, 2008: FEBS Letters
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