Structure Analysis of Entamoeba histolytica DNMT2 (EhMeth)

2012 | journal article???original???. A publication of Göttingen

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​Structure Analysis of Entamoeba histolytica DNMT2 (EhMeth)​
Schulz, E. C.; Roth, H. M.; Ankri, S. & Ficner, R. ​ (2012) 
PLoS ONE7(6) art. e38728​.​ DOI: https://doi.org/10.1371/journal.pone.0038728 

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Authors
Schulz, Eike Christian; Roth, Heide M.; Ankri, Serge; Ficner, Ralf 
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 angstrom, 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.
Issue Date
2012
Publisher
Public Library Science
Journal
PLoS ONE 
ISSN
1932-6203
Sponsor
Open-Access-Publikationsfonds 2012

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