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Chemical Evolution of a Bacterial Proteome |
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| Authors: | Dr Michael Georg Hoesl M Sc Stefan Oehm Dr Patrick Durkin Dr Elise Darmon Dr Lauri Peil Dr Hans‐Rudolf Aerni Prof Dr Juri Rappsilber Prof Dr Jesse Rinehart Prof Dr David Leach Prof Dr Dieter Söll Prof Dr Nediljko Budisa |
| Institution: | 1. Institut für Chemie, Technische Universit?t Berlin, Müller‐Breslau‐Strasse 10, 10623 Berlin (Germany);2. Institute of Cell Biology, School of Biological Sciences, University of Edinburgh (UK);3. Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, 4.17 Michael Swann Building, Edinburgh EH9 3BF (UK);4. Systems Biology Institute, Yale University, West Haven, CT 06516 (USA);5. Institut für Biotechnolgie, Technische Universit?t Berlin, Gustav‐Meyer‐Allee 25, 13355 Berlin (Germany);6. Department of Molecular Biophysics and Biochemistry and Department of Chemistry, Yale University, New Haven, CT 06520 (USA) |
| Abstract: | We have changed the amino acid set of the genetic code of Escherichia coli by evolving cultures capable of growing on the synthetic noncanonical amino acid L ‐β‐(thieno3,2‐b]pyrrolyl)alanine (3,2]Tpa) as a sole surrogate for the canonical amino acid L ‐tryptophan (Trp). A long‐term cultivation experiment in defined synthetic media resulted in the evolution of cells capable of surviving Trp→3,2]Tpa substitutions in their proteomes in response to the 20 899 TGG codons of the E. coli W3110 genome. These evolved bacteria with new‐to‐nature amino acid composition showed robust growth in the complete absence of Trp. Our experimental results illustrate an approach for the evolution of synthetic cells with alternative biochemical building blocks. |
| Keywords: | continuous evolution Escherichia coli genetic code translation synthetic biology tryptophan analogues |