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The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature
Aminoacyl tRNA synthetases primarily function to attach specific amino acids to the corresponding tRNAs during protein translation. However, their roles in regulating plant growth and development still remain elusive. Here we reported a rice thermo-sensitive mutant yellow leaf chlorosis3 (ylc3) with...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9635353/ https://www.ncbi.nlm.nih.gov/pubmed/36340382 http://dx.doi.org/10.3389/fpls.2022.847364 |
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author | Liu, Hongjia Gong, Xue Deng, Hui Tan, Jinjuan Sun, Yanqing Wang, Fang Wu, Wenjuan Zhou, Zhongjing Xu, Rumeng He, Haiyan Lo, Clive |
author_facet | Liu, Hongjia Gong, Xue Deng, Hui Tan, Jinjuan Sun, Yanqing Wang, Fang Wu, Wenjuan Zhou, Zhongjing Xu, Rumeng He, Haiyan Lo, Clive |
author_sort | Liu, Hongjia |
collection | PubMed |
description | Aminoacyl tRNA synthetases primarily function to attach specific amino acids to the corresponding tRNAs during protein translation. However, their roles in regulating plant growth and development still remain elusive. Here we reported a rice thermo-sensitive mutant yellow leaf chlorosis3 (ylc3) with reduced chlorophyll content, altered thylakoid structure, and substantially elevated levels of free aspartate, asparagine and glutamine in leaves under low temperature condition. Map-based cloning identified that YLC3 encodes an aspartyl-tRNA synthetase which is localized in cytosol and mitochondria. In addition, quantitative proteomics analysis revealed that both nuclear and chloroplast-encoded thylakoid proteins were significantly down-regulated in the mutant. On the other hand, proteins involved in amino acid metabolism and the process of protein synthesis were up-regulated in ylc3, particularly for key enzymes that convert aspartate to asparagine. Moreover, uncharged tRNA-Asp accumulation and phosphorylation of the translation initiation factor eIF2α was detected in the mutant, suggesting that YLC3 regulates the homeostasis of amino acid metabolism and chloroplast thylakoid development through modulation of processes during protein synthesis. |
format | Online Article Text |
id | pubmed-9635353 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-96353532022-11-05 The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature Liu, Hongjia Gong, Xue Deng, Hui Tan, Jinjuan Sun, Yanqing Wang, Fang Wu, Wenjuan Zhou, Zhongjing Xu, Rumeng He, Haiyan Lo, Clive Front Plant Sci Plant Science Aminoacyl tRNA synthetases primarily function to attach specific amino acids to the corresponding tRNAs during protein translation. However, their roles in regulating plant growth and development still remain elusive. Here we reported a rice thermo-sensitive mutant yellow leaf chlorosis3 (ylc3) with reduced chlorophyll content, altered thylakoid structure, and substantially elevated levels of free aspartate, asparagine and glutamine in leaves under low temperature condition. Map-based cloning identified that YLC3 encodes an aspartyl-tRNA synthetase which is localized in cytosol and mitochondria. In addition, quantitative proteomics analysis revealed that both nuclear and chloroplast-encoded thylakoid proteins were significantly down-regulated in the mutant. On the other hand, proteins involved in amino acid metabolism and the process of protein synthesis were up-regulated in ylc3, particularly for key enzymes that convert aspartate to asparagine. Moreover, uncharged tRNA-Asp accumulation and phosphorylation of the translation initiation factor eIF2α was detected in the mutant, suggesting that YLC3 regulates the homeostasis of amino acid metabolism and chloroplast thylakoid development through modulation of processes during protein synthesis. Frontiers Media S.A. 2022-03-04 /pmc/articles/PMC9635353/ /pubmed/36340382 http://dx.doi.org/10.3389/fpls.2022.847364 Text en Copyright © 2022 Liu, Gong, Deng, Tan, Sun, Wang, Wu, Zhou, Xu, He and Lo. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Liu, Hongjia Gong, Xue Deng, Hui Tan, Jinjuan Sun, Yanqing Wang, Fang Wu, Wenjuan Zhou, Zhongjing Xu, Rumeng He, Haiyan Lo, Clive The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature |
title | The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature |
title_full | The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature |
title_fullStr | The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature |
title_full_unstemmed | The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature |
title_short | The Rice Aspartyl-tRNA Synthetase YLC3 Regulates Amino Acid Homeostasis and Chloroplast Development Under Low Temperature |
title_sort | rice aspartyl-trna synthetase ylc3 regulates amino acid homeostasis and chloroplast development under low temperature |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9635353/ https://www.ncbi.nlm.nih.gov/pubmed/36340382 http://dx.doi.org/10.3389/fpls.2022.847364 |
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