ArticleNature communications2020
Distinct metabolic states of a cell guide alternate fates of mutational buffering through altered proteostasis.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Patient-derived cornea organoid model to study metabolomic characterization of rare disease: aniridia-associated keratopathy.BMC ophthalmology · 2025Article
- Rewiring of the protein-protein-metabolite interactome during the diauxic shift in yeast.Cellular and molecular life sciences : CMLS · 2022Article
- GroEL/S Overexpression Helps to Purge Deleterious Mutations and Reduce Genetic Diversity during Adaptive Protein Evolution.Molecular biology and evolution · 2022Article
- Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.G3 (Bethesda, Md.) · 2021Article
- Recent advances in understanding the role of proteostasis.Faculty reviews · 2021Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 3 countries.
Funding
Abstract
Metabolic changes alter the cellular milieu; can this also change intracellular protein folding? Since proteostasis can modulate mutational buffering, if change in metabolism has the ability to change protein folding, arguably, it should also alter mutational buffering. Here we find that altered cellular metabolic states in E. coli buffer distinct mutations on model proteins. Buffered-mutants have folding problems in vivo and are differently chaperoned in different metabolic states. Notably, this assistance is dependent upon the metabolites and not on the increase in canonical chaperone machineries. Being able to reconstitute the folding assistance afforded by metabolites in vitro, we propose that changes in metabolite concentrations have the potential to alter protein folding capacity. Collectively, we unravel that the metabolite pools are bona fide members of proteostasis and aid in mutational buffering. Given the plasticity in cellular metabolism, we posit that metabolic alterations may play an important role in cellular proteostasis.
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Registered trials
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