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Investigations of Single-Subunit tRNA Methyltransferases from Yeast
tRNA methylations, including base modification and 2’-O-methylation of ribose moiety, play critical roles in the structural stabilization of tRNAs and the fidelity and efficiency of protein translation. These modifications are catalyzed by tRNA methyltransferases (TRMs). Some of the TRMs from yeast...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10608323/ https://www.ncbi.nlm.nih.gov/pubmed/37888286 http://dx.doi.org/10.3390/jof9101030 |
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author | Wang, Zhongyuan Xu, Xiangbin Li, Xinhai Fang, Jiaqi Huang, Zhenkuai Zhang, Mengli Liu, Jiameng Qiu, Xiaoting |
author_facet | Wang, Zhongyuan Xu, Xiangbin Li, Xinhai Fang, Jiaqi Huang, Zhenkuai Zhang, Mengli Liu, Jiameng Qiu, Xiaoting |
author_sort | Wang, Zhongyuan |
collection | PubMed |
description | tRNA methylations, including base modification and 2’-O-methylation of ribose moiety, play critical roles in the structural stabilization of tRNAs and the fidelity and efficiency of protein translation. These modifications are catalyzed by tRNA methyltransferases (TRMs). Some of the TRMs from yeast can fully function only by a single subunit. In this study, after performing the primary bioinformatic analyses, the progress of the studies of yeast single-subunit TRMs, as well as the studies of their homologues from yeast and other types of eukaryotes and the corresponding TRMs from other types of organisms was systematically reviewed, which will facilitate the understanding of the evolutionary origin of functional diversity of eukaryotic single-subunit TRM. |
format | Online Article Text |
id | pubmed-10608323 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106083232023-10-28 Investigations of Single-Subunit tRNA Methyltransferases from Yeast Wang, Zhongyuan Xu, Xiangbin Li, Xinhai Fang, Jiaqi Huang, Zhenkuai Zhang, Mengli Liu, Jiameng Qiu, Xiaoting J Fungi (Basel) Review tRNA methylations, including base modification and 2’-O-methylation of ribose moiety, play critical roles in the structural stabilization of tRNAs and the fidelity and efficiency of protein translation. These modifications are catalyzed by tRNA methyltransferases (TRMs). Some of the TRMs from yeast can fully function only by a single subunit. In this study, after performing the primary bioinformatic analyses, the progress of the studies of yeast single-subunit TRMs, as well as the studies of their homologues from yeast and other types of eukaryotes and the corresponding TRMs from other types of organisms was systematically reviewed, which will facilitate the understanding of the evolutionary origin of functional diversity of eukaryotic single-subunit TRM. MDPI 2023-10-19 /pmc/articles/PMC10608323/ /pubmed/37888286 http://dx.doi.org/10.3390/jof9101030 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Wang, Zhongyuan Xu, Xiangbin Li, Xinhai Fang, Jiaqi Huang, Zhenkuai Zhang, Mengli Liu, Jiameng Qiu, Xiaoting Investigations of Single-Subunit tRNA Methyltransferases from Yeast |
title | Investigations of Single-Subunit tRNA Methyltransferases from Yeast |
title_full | Investigations of Single-Subunit tRNA Methyltransferases from Yeast |
title_fullStr | Investigations of Single-Subunit tRNA Methyltransferases from Yeast |
title_full_unstemmed | Investigations of Single-Subunit tRNA Methyltransferases from Yeast |
title_short | Investigations of Single-Subunit tRNA Methyltransferases from Yeast |
title_sort | investigations of single-subunit trna methyltransferases from yeast |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10608323/ https://www.ncbi.nlm.nih.gov/pubmed/37888286 http://dx.doi.org/10.3390/jof9101030 |
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