Multiomics Analysis Provides Insight into the Laboratory Evolution of <i>Escherichia coli</i> toward the Metabolic Usage of Fluorinated Indoles
Federica Agostini, Ludwig Sinn, Daniel Petras, Christian J. Schipp, Vladimir Kubyshkin, A. Berger, Pieter C. Dorrestein, Juri Rappsilber, Nediljko Budiša, Beate Koksch
Abstract
synthesis of Trp analogues, followed by their incorporation in the cellular proteome. We found that full adaptation to both fluorinated Trp analogues requires a low number of 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 behind the adaptation to unnatural amino acids and provide the molecular foundation for bioengineering of novel microbial strains for synthetic biology and biotechnology.
Topics & Concepts
Escherichia coliAmino acidSynthetic biologyProteomeBiochemistryBiologyChemistryComputational biologyGeneFluorine in Organic ChemistryBiochemical and Molecular ResearchRNA and protein synthesis mechanisms