Proteomics

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Laboratory evolution of Escherichia coli enables life based on fluorinated amino acids


ABSTRACT: Organofluorine compounds are toxic to various living beings in different habitats. This usher the development of strategies based on the metabolic capacity of various fast-growing microbial strains to evolve an effective adaptation strategy for efficient environmental cleaning. We tackle this problem by trying to answer an essential question: can fluorinated amino acids be used as xenobiotics in general to build up biomass, or do large amounts of fluorine in the cells render them nonviable? To gain information about the effect of long-term exposure of a cellular proteome to fluorine, we constructed an experimental model based on bacterial adaptation in artificial fluorinated habitats. In particular, we propagated Escherichia coli (E. coli) in the presence of either 4- or 5-fluoroindole as essential precursors for the in situ synthesis of tryptophan (Trp) analogues. We found that full adaptation requires astonishingly few genetic mutations but is accompanied by large rearrangements in regulatory networks, membrane integrity and quality control of protein folding. These findings highlight the cellular mechanisms of the evolutionary adaption process and provide the molecular foundation for novel and innovative bioengineering of microbial strains potentially useful in bioaugmentation in fluorine-contaminated areas.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Escherichia Coli

SUBMITTER: Ludwig Sinn  

LAB HEAD: Juri Rappsilber

PROVIDER: PXD011771 | Pride | 2020-11-24

REPOSITORIES: Pride

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