Abstract
AbstractAlthough the effect of temperature on microbial growth has been widely studied, the role of proteome allocation in bringing about temperature-induced changes remains elusive. To tackle this problem, we propose a coarse-grained model of microbial growth, including the processes of temperature-sensitive protein unfolding and chaperone-assisted (re)folding. We determine the proteome sector allocation that maximizes balanced growth rate as a function of nutrient limitation and temperature. Calibrated with quantitative proteomic data for Escherichia coli, the model allows us to clarify general principles of temperature-dependent proteome allocation and formulate generalized growth laws. The same activation energy for metabolic enzymes and ribosomes leads to an Arrhenius increase in growth rate at constant proteome composition over a large range of temperatures, whereas at extreme temperatures resources are diverted away from growth to chaperone-mediated stress responses. Our approach points at risks and possible remedies for the use of ribosome content to characterize complex ecosystems with temperature variation.
Funder
the FMJH Program PGMO (from EDF-THALES-ORANGE) and the INRIA Project Lab Algae in silico
the FMJH Program PGMO (from EDF-THALES-ORANGE), the INRIA Project Lab Algae in silico, and the ANR project Maximic
the INRIA Project Lab Algae in silico and the ANR project Maximic
Publisher
Springer Science and Business Media LLC
Subject
Applied Mathematics,Computer Science Applications,Drug Discovery,General Biochemistry, Genetics and Molecular Biology,Modelling and Simulation
Cited by
19 articles.
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