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Project

Evolutionary strategies for fine-tuning the heat resistance vs. growth trade-off in Escherichia coli

While aggregation of proteins inside the cells has been widely regarded as an adverse cellular phenomenon, our group and others have most recently shown counterintuitive positive cellular effects of protein aggregates in microorganisms. In fact, our preliminary results strongly suggest that adaptive evolution can capitalize on mutations that alter intracellular protein aggregation dynamics by sacrificing folding fidelity (either of a single protein or by a proteome-wide increase in ribosomal error rates), thereby enabling cells to preemptively trigger heat shock response that boosts the cell’s robustness on both the short term (i.e. through induction of the heat shock response) and the long term (i.e. through cross-generational inheritance of protein aggregates). We aim to elucidate whether and to which extent the deliberate sacrifice of protein folding fidelity is actually sampled as a significant adaptive mechanism in nature and how the selection of adaptation strategies is being influenced by environmental conditions.
Date:1 Dec 2020 →  31 Oct 2021
Keywords:proteostasis, heat stress, protein aggregates, evolution, growth speed
Disciplines:Bacteriology, Genetics, Cell physiology, Cell growth and development