ArticleJournal of bacteriology2012
Identification and characterization of a highly conserved crenarchaeal protein lysine methyltransferase with broad substrate specificity.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Protein methylation in mitochondria.The Journal of biological chemistry · 2022Review
- Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA.Frontiers in microbiology · 2022Article
- Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.PLoS pathogens · 2021Article
- Post-Translational Modifications Aid Archaeal Survival.Biomolecules · 2020Review
- Methylation deficiency of chromatin proteins is a non-mutational and epigenetic-like trait in evolved lines of the archaeonThe Journal of biological chemistry · 2019Article
- Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase.The Journal of biological chemistry · 2019Article
- Methylthioadenosine Suppresses Salmonella Virulence.Infection and immunity · 2018Article
- Article
- The extraordinary thermal stability of EstA from S. islandicus is independent of post translational modifications.Protein science : a publication of the Protein Society · 2017Article
- Abundant Lysine Methylation and N-Terminal Acetylation in Sulfolobus islandicus Revealed by Bottom-Up and Top-Down Proteomics.Molecular & cellular proteomics : MCP · 2016Article
- aKMT Catalyzes Extensive Protein Lysine Methylation in the Hyperthermophilic Archaeon Sulfolobus islandicus but is Dispensable for the Growth of the Organism.Molecular & cellular proteomics : MCP · 2016Article
- The Helicase Activity of Hyperthermophilic Archaeal MCM is Enhanced at High Temperatures by Lysine Methylation.Frontiers in microbiology · 2015Article
- An unexpected journey: lysine methylation across the proteome.Biochimica et biophysica acta · 2014Review
- Chromatin structure and dynamics in hot environments: architectural proteins and DNA topoisomerases of thermophilic archaea.International journal of molecular sciences · 2014Review
- The functional diversity of protein lysine methylation.Molecular systems biology · 2014Review
- Bacterial SET domain proteins and their role in eukaryotic chromatin modification.Frontiers in genetics · 2014Review
- A prototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns.The Journal of biological chemistry · 2013Article
- Protein methylation at the surface and buried deep: thinking outside the histone box.Trends in biochemical sciences · 2013Review
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein lysine methylation occurs extensively in the Crenarchaeota, a major kingdom in the Archaea. However, the enzymes responsible for this type of posttranslational modification have not been found. Here we report the identification and characterization of the first crenarchaeal protein lysine methyltransferase, designated aKMT, from the hyperthermophilic crenarchaeon Sulfolobus islandicus. The enzyme was capable of transferring methyl groups to selected lysine residues in a substrate protein using S-adenosyl-l-methionine (SAM) as the methyl donor. aKMT, a non-SET domain protein, is highly conserved among crenarchaea, and distantly related homologs also exist in Bacteria and Eukarya. aKMT was active over a wide range of temperatures, from ~25 to 90 °C, with an optimal temperature at ~60 to 70 °C. Amino acid residues Y9 and T12 at the N terminus appear to be the key residues in the putative active site of aKMT, as indicated by sequence conservation and site-directed mutagenesis. Although aKMT was identified based on its methylating activity on Cren7, the crenarchaeal chromatin protein, it exhibited broad substrate specificity and was capable of methylating a number of recombinant Sulfolobus proteins overproduced in Escherichia coli. The finding of aKMT will help elucidate mechanisms underlining extensive protein lysine methylation and the functional significance of posttranslational protein methylation in crenarchaea.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.