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Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures
Metazoan organisms have many tRNA genes responsible for decoding amino acids. The set of all tRNA genes can be grouped in sets of common amino acids and isoacceptor tRNAs that are aminoacylated by corresponding aminoacyl-tRNA synthetases. Analysis of tRNA alignments shows that, despite the high numb...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9023262/ https://www.ncbi.nlm.nih.gov/pubmed/35380696 http://dx.doi.org/10.1093/nar/gkac222 |
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author | Westhof, Eric Thornlow, Bryan Chan, Patricia P Lowe, Todd M |
author_facet | Westhof, Eric Thornlow, Bryan Chan, Patricia P Lowe, Todd M |
author_sort | Westhof, Eric |
collection | PubMed |
description | Metazoan organisms have many tRNA genes responsible for decoding amino acids. The set of all tRNA genes can be grouped in sets of common amino acids and isoacceptor tRNAs that are aminoacylated by corresponding aminoacyl-tRNA synthetases. Analysis of tRNA alignments shows that, despite the high number of tRNA genes, specific tRNA sequence motifs are highly conserved across multicellular eukaryotes. The conservation often extends throughout the isoacceptors and isodecoders with, in some cases, two sets of conserved isodecoders. This study is focused on non-Watson–Crick base pairs in the helical stems, especially GoU pairs. Each of the four helical stems may contain one or more conserved GoU pairs. Some are amino acid specific and could represent identity elements for the cognate aminoacyl tRNA synthetases. Other GoU pairs are found in more than a single amino acid and could be critical for native folding of the tRNAs. Interestingly, some GoU pairs are anticodon-specific, and others are found in phylogenetically-specific clades. Although the distribution of conservation likely reflects a balance between accommodating isotype-specific functions as well as those shared by all tRNAs essential for ribosomal translation, such conservations may indicate the existence of specialized tRNAs for specific translation targets, cellular conditions, or alternative functions. |
format | Online Article Text |
id | pubmed-9023262 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-90232622022-04-22 Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures Westhof, Eric Thornlow, Bryan Chan, Patricia P Lowe, Todd M Nucleic Acids Res RNA and RNA-protein complexes Metazoan organisms have many tRNA genes responsible for decoding amino acids. The set of all tRNA genes can be grouped in sets of common amino acids and isoacceptor tRNAs that are aminoacylated by corresponding aminoacyl-tRNA synthetases. Analysis of tRNA alignments shows that, despite the high number of tRNA genes, specific tRNA sequence motifs are highly conserved across multicellular eukaryotes. The conservation often extends throughout the isoacceptors and isodecoders with, in some cases, two sets of conserved isodecoders. This study is focused on non-Watson–Crick base pairs in the helical stems, especially GoU pairs. Each of the four helical stems may contain one or more conserved GoU pairs. Some are amino acid specific and could represent identity elements for the cognate aminoacyl tRNA synthetases. Other GoU pairs are found in more than a single amino acid and could be critical for native folding of the tRNAs. Interestingly, some GoU pairs are anticodon-specific, and others are found in phylogenetically-specific clades. Although the distribution of conservation likely reflects a balance between accommodating isotype-specific functions as well as those shared by all tRNAs essential for ribosomal translation, such conservations may indicate the existence of specialized tRNAs for specific translation targets, cellular conditions, or alternative functions. Oxford University Press 2022-04-05 /pmc/articles/PMC9023262/ /pubmed/35380696 http://dx.doi.org/10.1093/nar/gkac222 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | RNA and RNA-protein complexes Westhof, Eric Thornlow, Bryan Chan, Patricia P Lowe, Todd M Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures |
title | Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures |
title_full | Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures |
title_fullStr | Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures |
title_full_unstemmed | Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures |
title_short | Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures |
title_sort | eukaryotic trna sequences present conserved and amino acid-specific structural signatures |
topic | RNA and RNA-protein complexes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9023262/ https://www.ncbi.nlm.nih.gov/pubmed/35380696 http://dx.doi.org/10.1093/nar/gkac222 |
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