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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...

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Autores principales: Saga, Yusuke, Kawashima, Moeka, Sakai, Shiho, Yamazaki, Kaori, Kaneko, Misato, Takahashi, Moeka, Sato, Natsuko, Toyoda, Yohei, Takase, Shohei, Nakano, Takeshi, Kawakami, Naoto, Kushiro, Tetsuo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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.
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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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