ArticleChembiochem : a European journal of chemical biology2020
Lysine Ethylation by Histone Lysine Methyltransferases.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Histidine Ethylation by Histidine Methyltransferases SETD3 and METTL9.Chembiochem : a European journal of chemical biology · 2026Article
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- Write and Read: Harnessing Synthetic DNA Modifications for Nanopore Sequencing.bioRxiv : the preprint server for biology · 2025Article
- Inhibition of FBP1 expression by KMT5A through TWIST1 methylation is one of the mechanisms leading to chemoresistance in breast cancer.Oncology reports · 2024Article
- Tracking DOT1L methyltransferase activity by stable isotope labelling using a selective synthetic co-factor.Communications chemistry · 2024Article
- EBF2 Links KMT2D-Mediated H3K4me1 to Suppress Pancreatic Cancer Progression via Upregulating KLLN.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Sustained-release behavior and the antitumor effect of charge-convertible poly(amino acid)s drug-loaded nanoparticles.Drug delivery and translational research · 2023Article
- Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020Review
- Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases.Scientific reports · 2020Article
- Lysine Ethylation by Histone Lysine Methyltransferases.Chembiochem : a European journal of chemical biology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biomedicinally important histone lysine methyltransferases (KMTs) catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) cosubstrate to lysine residues in histones and other proteins. Herein, experimental and computational investigations on human KMT-catalyzed ethylation of histone peptides by using S-adenosylethionine (AdoEth) and Se-adenosylselenoethionine (AdoSeEth) cosubstrates are reported. MALDI-TOF MS experiments reveal that, unlike monomethyltransferases SETD7 and SETD8, methyltransferases G9a and G9a-like protein (GLP) do have the capacity to ethylate lysine residues in histone peptides, and that cosubstrates follow the efficiency trend AdoMet>AdoSeEth>AdoEth. G9a and GLP can also catalyze AdoSeEth-mediated ethylation of ornithine and produce histone peptides bearing lysine residues with different alkyl groups, such as H3K9meet and H3K9me2et. Molecular dynamics and free energy simulations based on quantum mechanics/molecular mechanics potential supported the experimental findings by providing an insight into the geometry and energetics of the enzymatic methyl/ethyl transfer process.
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