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

By Federica Agostini, Ludwig Sinn, Daniel Petras, Christian J. Schipp, Vladimir Kubyshkin, Allison Ann Berger, Pieter C. Dorrestein, Juri Rappsilber, Nediljko Budisa, Beate Koksch

Posted 10 Jun 2019
bioRxiv DOI: 10.1101/665950

Organofluorine compounds are toxic to various living beings in different habitats. On the other hand, fluorine incorporation into single proteins via related amino acid analogues has become common practice in protein engineering. Thus, an essential question remains: can fluorinated amino acids generally be used as xeno-nutrients 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 fluorinated organic compounds, we constructed an experiment based on bacterial adaptation in artificial fluorinated habitats. 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 to unnatural amino acids and provide the molecular foundation for novel and innovative bioengineering of microbial strains with potential for biotechnological applications.

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