ArticleThe Journal of biological chemistry2016
Substrate Specificity of the HEMK2 Protein Glutamine Methyltransferase and Identification of Novel Substrates.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- β-elemene promotes ferroptosis to improve the sensitivity of imatinib in gastrointestinal stromal tumours by targeting N6AMT1.Clinical and translational medicine · 2025Article
- Structure-Guided Design of a KMT9 Inhibitor Prodrug with Cellular Activity.Journal of medicinal chemistry · 2025Article
- CytosolicProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues.Protein science : a publication of the Protein Society · 2024Article
- The methyltransferase N6AMT1 participates in the cell cycle by regulating cyclin E levels.PloS one · 2024Article
- Shaping eukaryotic epigenetic systems by horizontal gene transfer.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Semisynthesis of Glutamine-Methylated Proteins Enabled by Genetic Code Expansion.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mammalian HEMK1 methylates glutamine residue of the GGQ motif of mitochondrial release factors.Scientific reports · 2022Article
- Bacterial N4-methylcytosine as an epigenetic mark in eukaryotic DNA.Nature communications · 2022Article
- Specificity Analysis of Protein Methyltransferases and Discovery of Novel Substrates Using SPOT Peptide Arrays.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Global analysis of protein arginine methylation.Cell reports methods · 2021Article
- Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease.Nature reviews. Drug discovery · 2021Review
- The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.Nucleic acids research · 2020Article
- An engineered variant of SETD3 methyltransferase alters target specificity from histidine to lysine methylation.The Journal of biological chemistry · 2020Article
- Posttranslational Methylation of Arginine in Methyl Coenzyme M Reductase Has a Profound Impact on both Methanogenesis and Growth of Methanococcus maripaludis.Journal of bacteriology · 2020Article
- The Common Partner of Several Methyltransferases TRMT112 Regulates the Expression of N6AMT1 Isoforms in Mammalian Cells.Biomolecules · 2019Article
- An Adversarial DNA NMolecular cell · 2019Article
- Structural insight into human N6amt1-Trm112 complex functioning as a protein methyltransferase.Cell discovery · 2019Article
- Human HemK2/KMT9/N6AMT1 is an active protein methyltransferase, but does not act on DNA in vitro, in the presence of Trm112.Cell discovery · 2019Article
- Systematic Functional Characterization of Human 21st Chromosome Orthologs inG3 (Bethesda, Md.) · 2018Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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. Our data show that HEMK2 requires a GQX3R motif for methylation activity. In addition, amino acid preferences were observed between the -3 and +7 positions of the peptide substrate (considering the target glutamine as 0), including a preference for Ser, Arg, and Gly at the +1 and a preference for Arg at the +7 position. Based on our specificity profile, we identified several human proteins that contain putative HEMK2 methylation sites and show that HEMK2 methylates 58 novel peptide substrates. After cloning, expression, and purification of the corresponding protein domains, we confirmed methylation for 11 of them at the protein level. Transfected CHD5 (chromodomain helicase DNA-binding protein 5) and NUT (nuclear protein in testis) were also demonstrated to be methylated by HEMK2 in human HEK293 cells. Our data expand the range of proteins potentially subjected to glutamine methylation significantly, but further investigation will be required to understand the function of HEMK2-mediated methylation in proteins other than eRF1.
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