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Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates

The 2′-O-methylation of the nucleoside at position 32 of tRNA is found in organisms belonging to the three domains of life. Unrelated enzymes catalyzing this modification in Bacteria (TrmJ) and Eukarya (Trm7) have already been identified, but until now, no information is available for the archaeal e...

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Autores principales: Somme, Jonathan, Van Laer, Bart, Roovers, Martine, Steyaert, Jan, Versées, Wim, Droogmans, Louis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4105751/
https://www.ncbi.nlm.nih.gov/pubmed/24951554
http://dx.doi.org/10.1261/rna.044503.114
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author Somme, Jonathan
Van Laer, Bart
Roovers, Martine
Steyaert, Jan
Versées, Wim
Droogmans, Louis
author_facet Somme, Jonathan
Van Laer, Bart
Roovers, Martine
Steyaert, Jan
Versées, Wim
Droogmans, Louis
author_sort Somme, Jonathan
collection PubMed
description The 2′-O-methylation of the nucleoside at position 32 of tRNA is found in organisms belonging to the three domains of life. Unrelated enzymes catalyzing this modification in Bacteria (TrmJ) and Eukarya (Trm7) have already been identified, but until now, no information is available for the archaeal enzyme. In this work we have identified the methyltransferase of the archaeon Sulfolobus acidocaldarius responsible for the 2′-O-methylation at position 32. This enzyme is a homolog of the bacterial TrmJ. Remarkably, both enzymes have different specificities for the nature of the nucleoside at position 32. While the four canonical nucleosides are substrates of the Escherichia coli enzyme, the archaeal TrmJ can only methylate the ribose of a cytidine. Moreover, the two enzymes recognize their tRNA substrates in a different way. We have solved the crystal structure of the catalytic domain of both enzymes to gain better understanding of these differences at a molecular level.
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spelling pubmed-41057512015-08-01 Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates Somme, Jonathan Van Laer, Bart Roovers, Martine Steyaert, Jan Versées, Wim Droogmans, Louis RNA Articles The 2′-O-methylation of the nucleoside at position 32 of tRNA is found in organisms belonging to the three domains of life. Unrelated enzymes catalyzing this modification in Bacteria (TrmJ) and Eukarya (Trm7) have already been identified, but until now, no information is available for the archaeal enzyme. In this work we have identified the methyltransferase of the archaeon Sulfolobus acidocaldarius responsible for the 2′-O-methylation at position 32. This enzyme is a homolog of the bacterial TrmJ. Remarkably, both enzymes have different specificities for the nature of the nucleoside at position 32. While the four canonical nucleosides are substrates of the Escherichia coli enzyme, the archaeal TrmJ can only methylate the ribose of a cytidine. Moreover, the two enzymes recognize their tRNA substrates in a different way. We have solved the crystal structure of the catalytic domain of both enzymes to gain better understanding of these differences at a molecular level. Cold Spring Harbor Laboratory Press 2014-08 /pmc/articles/PMC4105751/ /pubmed/24951554 http://dx.doi.org/10.1261/rna.044503.114 Text en © 2014 Somme et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Articles
Somme, Jonathan
Van Laer, Bart
Roovers, Martine
Steyaert, Jan
Versées, Wim
Droogmans, Louis
Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates
title Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates
title_full Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates
title_fullStr Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates
title_full_unstemmed Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates
title_short Characterization of two homologous 2′-O-methyltransferases showing different specificities for their tRNA substrates
title_sort characterization of two homologous 2′-o-methyltransferases showing different specificities for their trna substrates
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4105751/
https://www.ncbi.nlm.nih.gov/pubmed/24951554
http://dx.doi.org/10.1261/rna.044503.114
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