Chemical evolution of a bacterial proteome

Michael Georg Hoesl, Stefan Oehm, Patrick Durkin, Elise Darmon, Lauri Peil, Hans-Rudolf Aerni, Juri Rappsilber, Jesse Rinehart, David Leach, Dieter Söll, Nediljko Budisa

Research output: Contribution to journalArticlepeer-review


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-(thieno[3,2-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.

Original languageEnglish
Pages (from-to)10030-10034
Number of pages5
JournalAngewandte Chemie International Edition
Issue number34
Early online date1 Jul 2015
Publication statusPublished - 17 Aug 2015


  • alanine
  • bridged bicyclo compounds
  • escherichia coli
  • escherichia coli proteins
  • evolution
  • proteome
  • chemical
  • heterocyclic
  • analogs & derivatives

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