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A threonyl-tRNA synthetase-mediated translation initiation machinery
A fundamental question in biology is how vertebrates evolved and differ from invertebrates, and little is known about differences in the regulation of translation in the two systems. Herein, we identify a threonyl-tRNA synthetase (TRS)-mediated translation initiation machinery that specifically inte...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6430810/ https://www.ncbi.nlm.nih.gov/pubmed/30902983 http://dx.doi.org/10.1038/s41467-019-09086-0 |
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author | Jeong, Seung Jae Park, Shinhye Nguyen, Loi T. Hwang, Jungwon Lee, Eun-Young Giong, Hoi-Khoanh Lee, Jeong-Soo Yoon, Ina Lee, Ji-Hyun Kim, Jong Hyun Kim, Hoi Kyoung Kim, Doyeun Yang, Won Suk Kim, Seon-Young Lee, Chan Yong Yu, Kweon Sonenberg, Nahum Kim, Myung Hee Kim, Sunghoon |
author_facet | Jeong, Seung Jae Park, Shinhye Nguyen, Loi T. Hwang, Jungwon Lee, Eun-Young Giong, Hoi-Khoanh Lee, Jeong-Soo Yoon, Ina Lee, Ji-Hyun Kim, Jong Hyun Kim, Hoi Kyoung Kim, Doyeun Yang, Won Suk Kim, Seon-Young Lee, Chan Yong Yu, Kweon Sonenberg, Nahum Kim, Myung Hee Kim, Sunghoon |
author_sort | Jeong, Seung Jae |
collection | PubMed |
description | A fundamental question in biology is how vertebrates evolved and differ from invertebrates, and little is known about differences in the regulation of translation in the two systems. Herein, we identify a threonyl-tRNA synthetase (TRS)-mediated translation initiation machinery that specifically interacts with eIF4E homologous protein, and forms machinery that is structurally analogous to the eIF4F-mediated translation initiation machinery via the recruitment of other translation initiation components. Biochemical and RNA immunoprecipitation analyses coupled to sequencing suggest that this machinery emerged as a gain-of-function event in the vertebrate lineage, and it positively regulates the translation of mRNAs required for vertebrate development. Collectively, our findings demonstrate that TRS evolved to regulate vertebrate translation initiation via its dual role as a scaffold for the assembly of initiation components and as a selector of target mRNAs. This work highlights the functional significance of aminoacyl-tRNA synthetases in the emergence and control of higher order organisms. |
format | Online Article Text |
id | pubmed-6430810 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-64308102019-03-25 A threonyl-tRNA synthetase-mediated translation initiation machinery Jeong, Seung Jae Park, Shinhye Nguyen, Loi T. Hwang, Jungwon Lee, Eun-Young Giong, Hoi-Khoanh Lee, Jeong-Soo Yoon, Ina Lee, Ji-Hyun Kim, Jong Hyun Kim, Hoi Kyoung Kim, Doyeun Yang, Won Suk Kim, Seon-Young Lee, Chan Yong Yu, Kweon Sonenberg, Nahum Kim, Myung Hee Kim, Sunghoon Nat Commun Article A fundamental question in biology is how vertebrates evolved and differ from invertebrates, and little is known about differences in the regulation of translation in the two systems. Herein, we identify a threonyl-tRNA synthetase (TRS)-mediated translation initiation machinery that specifically interacts with eIF4E homologous protein, and forms machinery that is structurally analogous to the eIF4F-mediated translation initiation machinery via the recruitment of other translation initiation components. Biochemical and RNA immunoprecipitation analyses coupled to sequencing suggest that this machinery emerged as a gain-of-function event in the vertebrate lineage, and it positively regulates the translation of mRNAs required for vertebrate development. Collectively, our findings demonstrate that TRS evolved to regulate vertebrate translation initiation via its dual role as a scaffold for the assembly of initiation components and as a selector of target mRNAs. This work highlights the functional significance of aminoacyl-tRNA synthetases in the emergence and control of higher order organisms. Nature Publishing Group UK 2019-03-22 /pmc/articles/PMC6430810/ /pubmed/30902983 http://dx.doi.org/10.1038/s41467-019-09086-0 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Jeong, Seung Jae Park, Shinhye Nguyen, Loi T. Hwang, Jungwon Lee, Eun-Young Giong, Hoi-Khoanh Lee, Jeong-Soo Yoon, Ina Lee, Ji-Hyun Kim, Jong Hyun Kim, Hoi Kyoung Kim, Doyeun Yang, Won Suk Kim, Seon-Young Lee, Chan Yong Yu, Kweon Sonenberg, Nahum Kim, Myung Hee Kim, Sunghoon A threonyl-tRNA synthetase-mediated translation initiation machinery |
title | A threonyl-tRNA synthetase-mediated translation initiation machinery |
title_full | A threonyl-tRNA synthetase-mediated translation initiation machinery |
title_fullStr | A threonyl-tRNA synthetase-mediated translation initiation machinery |
title_full_unstemmed | A threonyl-tRNA synthetase-mediated translation initiation machinery |
title_short | A threonyl-tRNA synthetase-mediated translation initiation machinery |
title_sort | threonyl-trna synthetase-mediated translation initiation machinery |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6430810/ https://www.ncbi.nlm.nih.gov/pubmed/30902983 http://dx.doi.org/10.1038/s41467-019-09086-0 |
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