Structural systems biology evaluation of metabolic thermotolerance in Escherichia coli.
Science, 2013/6/07;340(6137):1220-3.
Chang RL[1], Andrews K, Kim D, Li Z, Godzik A, Palsson BO
Affiliations
PMID: 23744946DOI: 10.1126/science.1234012
Impact factor: 63.714
Abstract
Genome-scale network reconstruction has enabled predictive modeling of metabolism for many systems. Traditionally, protein structural information has not been represented in such reconstructions. Expansion of a genome-scale model of Escherichia coli metabolism by including experimental and predicted protein structures enabled the analysis of protein thermostability in a network context. This analysis allowed the prediction of protein activities that limit network function at superoptimal temperatures and mechanistic interpretations of mutations found in strains adapted to heat. Predicted growth-limiting factors for thermotolerance were validated through nutrient supplementation experiments and defined metabolic sensitivities to heat stress, providing evidence that metabolic enzyme thermostability is rate-limiting at superoptimal temperatures. Inclusion of structural information expanded the content and predictive capability of genome-scale metabolic networks that enable structural systems biology of metabolism.
MeSH terms
Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Hot Temperature; Metabolic Networks and Pathways; Models, Biological; Protein Conformation; Systems Biology; Transcriptional Activation
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