M.A. Rubio
Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress
Rubio, M.A.; Napolitano, M.; Ochoa de Alda, J.A.G.; Santamaría-Gómez, J.; Patterson, C.J.; Foster, A.W.; Bru-Martínez, R.; Robinson, N.J.; Luque, I.
Authors
M. Napolitano
J.A.G. Ochoa de Alda
J. Santamaría-Gómez
C.J. Patterson
A.W. Foster
R. Bru-Martínez
Professor Nigel Robinson nigel.robinson@durham.ac.uk
Professor
I. Luque
Abstract
Aminoacyl-tRNA synthetases (aaRSs) play a key role in deciphering the genetic message by producing charged tRNAs and are equipped with proofreading mechanisms to ensure correct pairing of tRNAs with their cognate amino acid. Duplicated aaRSs are very frequent in Nature, with 25,913 cases observed in 26,837 genomes. The oligomeric nature of many aaRSs raises the question of how the functioning and oligomerization of duplicated enzymes is organized. We characterized this issue in a model prokaryotic organism that expresses two different threonyl-tRNA synthetases, responsible for Thr-tRNAThr synthesis: one accurate and constitutively expressed (T1) and another (T2) with impaired proofreading activity that also generates mischarged Ser-tRNAThr. Low zinc promotes dissociation of dimeric T1 into monomers deprived of aminoacylation activity and simultaneous induction of T2, which is active for aminoacylation under low zinc. T2 either forms homodimers or heterodimerizes with T1 subunits that provide essential proofreading activity in trans. These findings evidence that in organisms with duplicated genes, cells can orchestrate the assemblage of aaRSs oligomers that meet the necessities of the cell in each situation. We propose that controlled oligomerization of duplicated aaRSs is an adaptive mechanism that can potentially be expanded to the plethora of organisms with duplicated oligomeric aaRSs.
Citation
Rubio, M., Napolitano, M., Ochoa de Alda, J., Santamaría-Gómez, J., Patterson, C., Foster, A., …Luque, I. (2015). Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress. Nucleic Acids Research, 43(20), 9905-9917. https://doi.org/10.1093/nar/gkv1020
Journal Article Type | Article |
---|---|
Acceptance Date | Sep 28, 2015 |
Online Publication Date | Oct 12, 2015 |
Publication Date | Nov 16, 2015 |
Deposit Date | Oct 15, 2015 |
Publicly Available Date | Apr 7, 2016 |
Journal | Nucleic Acids Research |
Print ISSN | 0305-1048 |
Electronic ISSN | 1362-4962 |
Publisher | Oxford University Press |
Peer Reviewed | Peer Reviewed |
Volume | 43 |
Issue | 20 |
Pages | 9905-9917 |
DOI | https://doi.org/10.1093/nar/gkv1020 |
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Copyright Statement
© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
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