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Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures

All organisms universally encode, synthesize and utilize proteins that function optimally within a subset of growth conditions. While healthy cells are thought to maintain high translational fidelity within their natural habitats, natural environments can easily fluctuate outside the optimal functio...

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Autores principales: Schwartz, Michael H., Pan, Tao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705672/
https://www.ncbi.nlm.nih.gov/pubmed/26657639
http://dx.doi.org/10.1093/nar/gkv1379
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author Schwartz, Michael H.
Pan, Tao
author_facet Schwartz, Michael H.
Pan, Tao
author_sort Schwartz, Michael H.
collection PubMed
description All organisms universally encode, synthesize and utilize proteins that function optimally within a subset of growth conditions. While healthy cells are thought to maintain high translational fidelity within their natural habitats, natural environments can easily fluctuate outside the optimal functional range of genetically encoded proteins. The hyperthermophilic archaeon Aeropyrum pernix (A. pernix) can grow throughout temperature variations ranging from 70 to 100°C, although the specific factors facilitating such adaptability are unknown. Here, we show that A. pernix undergoes constitutive leucine to methionine mistranslation at low growth temperatures. Low-temperature mistranslation is facilitated by the misacylation of tRNA(Leu) with methionine by the methionyl-tRNA synthetase (MetRS). At low growth temperatures, the A. pernix MetRS undergoes a temperature dependent shift in tRNA charging fidelity, allowing the enzyme to conditionally charge tRNA(Leu) with methionine. We demonstrate enhanced low-temperature activity for A. pernix citrate synthase that is synthesized during leucine to methionine mistranslation at low-temperature growth compared to its high-fidelity counterpart synthesized at high-temperature. Our results show that conditional leucine to methionine mistranslation can make protein adjustments capable of improving the low-temperature activity of hyperthermophilic proteins, likely by facilitating the increasing flexibility required for greater protein function at lower physiological temperatures.
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spelling pubmed-47056722016-01-11 Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures Schwartz, Michael H. Pan, Tao Nucleic Acids Res Molecular Biology All organisms universally encode, synthesize and utilize proteins that function optimally within a subset of growth conditions. While healthy cells are thought to maintain high translational fidelity within their natural habitats, natural environments can easily fluctuate outside the optimal functional range of genetically encoded proteins. The hyperthermophilic archaeon Aeropyrum pernix (A. pernix) can grow throughout temperature variations ranging from 70 to 100°C, although the specific factors facilitating such adaptability are unknown. Here, we show that A. pernix undergoes constitutive leucine to methionine mistranslation at low growth temperatures. Low-temperature mistranslation is facilitated by the misacylation of tRNA(Leu) with methionine by the methionyl-tRNA synthetase (MetRS). At low growth temperatures, the A. pernix MetRS undergoes a temperature dependent shift in tRNA charging fidelity, allowing the enzyme to conditionally charge tRNA(Leu) with methionine. We demonstrate enhanced low-temperature activity for A. pernix citrate synthase that is synthesized during leucine to methionine mistranslation at low-temperature growth compared to its high-fidelity counterpart synthesized at high-temperature. Our results show that conditional leucine to methionine mistranslation can make protein adjustments capable of improving the low-temperature activity of hyperthermophilic proteins, likely by facilitating the increasing flexibility required for greater protein function at lower physiological temperatures. Oxford University Press 2016-01-08 2015-12-10 /pmc/articles/PMC4705672/ /pubmed/26657639 http://dx.doi.org/10.1093/nar/gkv1379 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 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 Molecular Biology
Schwartz, Michael H.
Pan, Tao
Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
title Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
title_full Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
title_fullStr Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
title_full_unstemmed Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
title_short Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
title_sort temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures
topic Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705672/
https://www.ncbi.nlm.nih.gov/pubmed/26657639
http://dx.doi.org/10.1093/nar/gkv1379
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