ArticlePloS one2012
Structure analysis of Entamoeba histolytica DNMT2 (EhMeth).
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Dissecting the function of the DNMT2-homolog (DNMA) in Dictyostelium discoideum.G3 (Bethesda, Md.) · 2025Article
- Prediction of diabetes mellitus after kidney transplantation using patient-specific induced pluripotent stem cells.Kidney research and clinical practice · 2024Article
- Advances in Protozoan Epigenetic Targets and Their Inhibitors for the Development of New Potential Drugs.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Determinants of DNMT2/TRDMT1 preference for substrates tRNA and DNA during the evolution.RNA biology · 2023Article
- New substrates and determinants for tRNA recognition of RNA methyltransferase DNMT2/TRDMT1.RNA biology · 2021Article
- RNA 5-methylcytosine modification and its emerging role as an epitranscriptomic mark.RNA biology · 2021Review
- Article
- A rationale for tRNA modification circuits in the anticodon loop.RNA (New York, N.Y.) · 2018Review
- Structural insights into the stimulation of S. pombe Dnmt2 catalytic efficiency by the tRNA nucleoside queuosine.Scientific reports · 2018Article
- Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation.RNA biology · 2017Review
- Widespread 5-methylcytosine in the genomes of avian Coccidia and other apicomplexan parasites detected by an ELISA-based method.Parasitology research · 2017Article
- Review
- Article
- The Entamoeba histolytica Dnmt2 homolog (Ehmeth) confers resistance to nitrosative stress.Eukaryotic cell · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, DNA methylation is an important epigenetic modification that is generally involved in gene regulation. Methyltransferases (MTases) of the DNMT2 family have been shown to have a dual substrate specificity acting on DNA as well as on three specific tRNAs (tRNA(Asp), tRNA(Val), tRNA(Gly)). Entamoeba histolytica is a major human pathogen, and expresses a single DNA MTase (EhMeth) that belongs to the DNMT2 family and shows high homology to the human enzyme as well as to the bacterial DNA MTase M.HhaI. The molecular basis for the recognition of the substrate tRNAs and discrimination of non-cognate tRNAs is unknown. Here we present the crystal structure of the cytosine-5-methyltransferase EhMeth at a resolution of 2.15 Å, in complex with its reaction product S-adenosyl-L-homocysteine, revealing all parts of a DNMT2 MTase, including the active site loop. Mobility shift assays show that in vitro the full length tRNA is required for stable complex formation with EhMeth.
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