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Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases
Aminoacyl-tRNA synthetases (aaRSs) play essential roles in protein translation. In addition, numerous aaRSs (mostly in vertebrates) have also been discovered to possess a range of non-canonical functions. Very few studies have been conducted to elucidate or characterize non-canonical functions of pl...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7564348/ https://www.ncbi.nlm.nih.gov/pubmed/32906706 http://dx.doi.org/10.3390/genes11091056 |
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author | Saga, Yusuke Kawashima, Moeka Sakai, Shiho Yamazaki, Kaori Kaneko, Misato Takahashi, Moeka Sato, Natsuko Toyoda, Yohei Takase, Shohei Nakano, Takeshi Kawakami, Naoto Kushiro, Tetsuo |
author_facet | Saga, Yusuke Kawashima, Moeka Sakai, Shiho Yamazaki, Kaori Kaneko, Misato Takahashi, Moeka Sato, Natsuko Toyoda, Yohei Takase, Shohei Nakano, Takeshi Kawakami, Naoto Kushiro, Tetsuo |
author_sort | Saga, Yusuke |
collection | PubMed |
description | Aminoacyl-tRNA synthetases (aaRSs) play essential roles in protein translation. In addition, numerous aaRSs (mostly in vertebrates) have also been discovered to possess a range of non-canonical functions. Very few studies have been conducted to elucidate or characterize non-canonical functions of plant aaRSs. A genome-wide search for aaRS genes in Arabidopsis thaliana revealed a total of 59 aaRS genes. Among them, asparaginyl-tRNA synthetase (AsnRS) was found to possess a WHEP domain inserted into the catalytic domain in a plant-specific manner. This insertion was observed only in the cytosolic isoform. In addition, a long stretch of sequence that exhibited weak homology with histidine ammonia lyase (HAL) was found at the N-terminus of histidyl-tRNA synthetase (HisRS). This HAL-like domain has only been seen in plant HisRS, and only in cytosolic isoforms. Additionally, a number of genes lacking minor or major portions of the full-length aaRS sequence were found. These genes encode 14 aaRS fragments that lack key active site sequences and are likely catalytically null. These identified genes that encode plant-specific additional domains or aaRS fragment sequences are candidates for aaRSs possessing non-canonical functions. |
format | Online Article Text |
id | pubmed-7564348 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-75643482020-10-26 Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases Saga, Yusuke Kawashima, Moeka Sakai, Shiho Yamazaki, Kaori Kaneko, Misato Takahashi, Moeka Sato, Natsuko Toyoda, Yohei Takase, Shohei Nakano, Takeshi Kawakami, Naoto Kushiro, Tetsuo Genes (Basel) Article Aminoacyl-tRNA synthetases (aaRSs) play essential roles in protein translation. In addition, numerous aaRSs (mostly in vertebrates) have also been discovered to possess a range of non-canonical functions. Very few studies have been conducted to elucidate or characterize non-canonical functions of plant aaRSs. A genome-wide search for aaRS genes in Arabidopsis thaliana revealed a total of 59 aaRS genes. Among them, asparaginyl-tRNA synthetase (AsnRS) was found to possess a WHEP domain inserted into the catalytic domain in a plant-specific manner. This insertion was observed only in the cytosolic isoform. In addition, a long stretch of sequence that exhibited weak homology with histidine ammonia lyase (HAL) was found at the N-terminus of histidyl-tRNA synthetase (HisRS). This HAL-like domain has only been seen in plant HisRS, and only in cytosolic isoforms. Additionally, a number of genes lacking minor or major portions of the full-length aaRS sequence were found. These genes encode 14 aaRS fragments that lack key active site sequences and are likely catalytically null. These identified genes that encode plant-specific additional domains or aaRS fragment sequences are candidates for aaRSs possessing non-canonical functions. MDPI 2020-09-07 /pmc/articles/PMC7564348/ /pubmed/32906706 http://dx.doi.org/10.3390/genes11091056 Text en © 2020 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 | Article Saga, Yusuke Kawashima, Moeka Sakai, Shiho Yamazaki, Kaori Kaneko, Misato Takahashi, Moeka Sato, Natsuko Toyoda, Yohei Takase, Shohei Nakano, Takeshi Kawakami, Naoto Kushiro, Tetsuo Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases |
title | Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases |
title_full | Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases |
title_fullStr | Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases |
title_full_unstemmed | Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases |
title_short | Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases |
title_sort | plant-specific domains and fragmented sequences imply non-canonical functions in plant aminoacyl-trna synthetases |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7564348/ https://www.ncbi.nlm.nih.gov/pubmed/32906706 http://dx.doi.org/10.3390/genes11091056 |
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