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Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains
Although more and more entangled participants of translation process were realized, how they cooperate and co-determine the final translation efficiency still lacks details. Here, we reasoned that the basic translation components, tRNAs and amino acids should be consistent to maximize the efficiency...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5726483/ https://www.ncbi.nlm.nih.gov/pubmed/28992099 http://dx.doi.org/10.1093/dnares/dsx030 |
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author | Du, Meng-Ze Wei, Wen Qin, Lei Liu, Shuo Zhang, An-Ying Zhang, Yong Zhou, Hong Guo, Feng-Biao |
author_facet | Du, Meng-Ze Wei, Wen Qin, Lei Liu, Shuo Zhang, An-Ying Zhang, Yong Zhou, Hong Guo, Feng-Biao |
author_sort | Du, Meng-Ze |
collection | PubMed |
description | Although more and more entangled participants of translation process were realized, how they cooperate and co-determine the final translation efficiency still lacks details. Here, we reasoned that the basic translation components, tRNAs and amino acids should be consistent to maximize the efficiency and minimize the cost. We firstly revealed that 310 out of 410 investigated genomes of three domains had significant co-adaptions between the tRNA gene copy numbers and amino acid compositions, indicating that maximum efficiency constitutes ubiquitous selection pressure on protein translation. Furthermore, fast-growing and larger bacteria are found to have significantly better co-adaption and confirmed the effect of this pressure. Within organism, highly expressed proteins and those connected to acute responses have higher co-adaption intensity. Thus, the better co-adaption probably speeds up the growing of cells through accelerating the translation of special proteins. Experimentally, manipulating the tRNA gene copy number to optimize co-adaption between enhanced green fluorescent protein (EGFP) and tRNA gene set of Escherichia coli indeed lifted the translation rate (speed). Finally, as a newly confirmed translation rate regulating mechanism, the co-adaption reflecting translation rate not only deepens our understanding on translation process but also provides an easy and practicable method to improve protein translation rates and productivity. |
format | Online Article Text |
id | pubmed-5726483 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-57264832017-12-18 Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains Du, Meng-Ze Wei, Wen Qin, Lei Liu, Shuo Zhang, An-Ying Zhang, Yong Zhou, Hong Guo, Feng-Biao DNA Res Full Papers Although more and more entangled participants of translation process were realized, how they cooperate and co-determine the final translation efficiency still lacks details. Here, we reasoned that the basic translation components, tRNAs and amino acids should be consistent to maximize the efficiency and minimize the cost. We firstly revealed that 310 out of 410 investigated genomes of three domains had significant co-adaptions between the tRNA gene copy numbers and amino acid compositions, indicating that maximum efficiency constitutes ubiquitous selection pressure on protein translation. Furthermore, fast-growing and larger bacteria are found to have significantly better co-adaption and confirmed the effect of this pressure. Within organism, highly expressed proteins and those connected to acute responses have higher co-adaption intensity. Thus, the better co-adaption probably speeds up the growing of cells through accelerating the translation of special proteins. Experimentally, manipulating the tRNA gene copy number to optimize co-adaption between enhanced green fluorescent protein (EGFP) and tRNA gene set of Escherichia coli indeed lifted the translation rate (speed). Finally, as a newly confirmed translation rate regulating mechanism, the co-adaption reflecting translation rate not only deepens our understanding on translation process but also provides an easy and practicable method to improve protein translation rates and productivity. Oxford University Press 2017-12 2017-07-11 /pmc/articles/PMC5726483/ /pubmed/28992099 http://dx.doi.org/10.1093/dnares/dsx030 Text en © The Author 2017. Published by Oxford University Press on behalf of Kazusa DNA Research Institute. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Full Papers Du, Meng-Ze Wei, Wen Qin, Lei Liu, Shuo Zhang, An-Ying Zhang, Yong Zhou, Hong Guo, Feng-Biao Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains |
title | Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains |
title_full | Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains |
title_fullStr | Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains |
title_full_unstemmed | Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains |
title_short | Co-adaption of tRNA gene copy number and amino acid usage influences translation rates in three life domains |
title_sort | co-adaption of trna gene copy number and amino acid usage influences translation rates in three life domains |
topic | Full Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5726483/ https://www.ncbi.nlm.nih.gov/pubmed/28992099 http://dx.doi.org/10.1093/dnares/dsx030 |
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