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Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA
To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially i...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6313347/ https://www.ncbi.nlm.nih.gov/pubmed/30347855 http://dx.doi.org/10.3390/microorganisms6040110 |
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author | Hori, Hiroyuki Kawamura, Takuya Awai, Takako Ochi, Anna Yamagami, Ryota Tomikawa, Chie Hirata, Akira |
author_facet | Hori, Hiroyuki Kawamura, Takuya Awai, Takako Ochi, Anna Yamagami, Ryota Tomikawa, Chie Hirata, Akira |
author_sort | Hori, Hiroyuki |
collection | PubMed |
description | To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science. |
format | Online Article Text |
id | pubmed-6313347 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63133472019-01-04 Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA Hori, Hiroyuki Kawamura, Takuya Awai, Takako Ochi, Anna Yamagami, Ryota Tomikawa, Chie Hirata, Akira Microorganisms Review To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science. MDPI 2018-10-20 /pmc/articles/PMC6313347/ /pubmed/30347855 http://dx.doi.org/10.3390/microorganisms6040110 Text en © 2018 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Hori, Hiroyuki Kawamura, Takuya Awai, Takako Ochi, Anna Yamagami, Ryota Tomikawa, Chie Hirata, Akira Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA |
title | Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA |
title_full | Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA |
title_fullStr | Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA |
title_full_unstemmed | Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA |
title_short | Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA |
title_sort | transfer rna modification enzymes from thermophiles and their modified nucleosides in trna |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6313347/ https://www.ncbi.nlm.nih.gov/pubmed/30347855 http://dx.doi.org/10.3390/microorganisms6040110 |
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