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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
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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. |
format | Online Article Text |
id | pubmed-3554419 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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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