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Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?

BACKGROUND: Temperature strongly affects microbial growth, and many microorganisms have to deal with temperature fluctuations in their natural environment. To understand regulation strategies that underlie microbial temperature responses and adaptation, we studied glycolytic pathway kinetics in Sacc...

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Autores principales: Cruz, Ana Luisa B, Hebly, Marit, Duong, Giang-Huong, Wahl, Sebastian A, Pronk, Jack T, Heijnen, Joseph J, Daran-Lapujade, Pascale, van Gulik, Walter M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3554419/
https://www.ncbi.nlm.nih.gov/pubmed/23216813
http://dx.doi.org/10.1186/1752-0509-6-151
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author Cruz, Ana Luisa B
Hebly, Marit
Duong, Giang-Huong
Wahl, Sebastian A
Pronk, Jack T
Heijnen, Joseph J
Daran-Lapujade, Pascale
van Gulik, Walter M
author_facet Cruz, Ana Luisa B
Hebly, Marit
Duong, Giang-Huong
Wahl, Sebastian A
Pronk, Jack T
Heijnen, Joseph J
Daran-Lapujade, Pascale
van Gulik, Walter M
author_sort Cruz, Ana Luisa B
collection PubMed
description BACKGROUND: Temperature strongly affects microbial growth, and many microorganisms have to deal with temperature fluctuations in their natural environment. To understand regulation strategies that underlie microbial temperature responses and adaptation, we studied glycolytic pathway kinetics in Saccharomyces cerevisiae during temperature changes. RESULTS: Saccharomyces cerevisiae was grown under different temperature regimes and glucose availability conditions. These included glucose-excess batch cultures at different temperatures and glucose-limited chemostat cultures, subjected to fast linear temperature shifts and circadian sinoidal temperature cycles. An observed temperature-independent relation between intracellular levels of glycolytic metabolites and residual glucose concentration for all experimental conditions revealed that it is the substrate availability rather than temperature that determines intracellular metabolite profiles. This observation corresponded with predictions generated in silico with a kinetic model of yeast glycolysis, when the catalytic capacities of all glycolytic enzymes were set to share the same normalized temperature dependency. CONCLUSIONS: From an evolutionary perspective, such similar temperature dependencies allow cells to adapt more rapidly to temperature changes, because they result in minimal perturbations of intracellular metabolite levels, thus circumventing the need for extensive modification of enzyme levels.
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spelling pubmed-35544192013-08-19 Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics? Cruz, Ana Luisa B Hebly, Marit Duong, Giang-Huong Wahl, Sebastian A Pronk, Jack T Heijnen, Joseph J Daran-Lapujade, Pascale van Gulik, Walter M BMC Syst Biol Research Article BACKGROUND: Temperature strongly affects microbial growth, and many microorganisms have to deal with temperature fluctuations in their natural environment. To understand regulation strategies that underlie microbial temperature responses and adaptation, we studied glycolytic pathway kinetics in Saccharomyces cerevisiae during temperature changes. RESULTS: Saccharomyces cerevisiae was grown under different temperature regimes and glucose availability conditions. These included glucose-excess batch cultures at different temperatures and glucose-limited chemostat cultures, subjected to fast linear temperature shifts and circadian sinoidal temperature cycles. An observed temperature-independent relation between intracellular levels of glycolytic metabolites and residual glucose concentration for all experimental conditions revealed that it is the substrate availability rather than temperature that determines intracellular metabolite profiles. This observation corresponded with predictions generated in silico with a kinetic model of yeast glycolysis, when the catalytic capacities of all glycolytic enzymes were set to share the same normalized temperature dependency. CONCLUSIONS: From an evolutionary perspective, such similar temperature dependencies allow cells to adapt more rapidly to temperature changes, because they result in minimal perturbations of intracellular metabolite levels, thus circumventing the need for extensive modification of enzyme levels. BioMed Central 2012-12-07 /pmc/articles/PMC3554419/ /pubmed/23216813 http://dx.doi.org/10.1186/1752-0509-6-151 Text en Copyright © 2012 Cruz et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Cruz, Ana Luisa B
Hebly, Marit
Duong, Giang-Huong
Wahl, Sebastian A
Pronk, Jack T
Heijnen, Joseph J
Daran-Lapujade, Pascale
van Gulik, Walter M
Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
title Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
title_full Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
title_fullStr Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
title_full_unstemmed Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
title_short Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
title_sort similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3554419/
https://www.ncbi.nlm.nih.gov/pubmed/23216813
http://dx.doi.org/10.1186/1752-0509-6-151
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