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Angew Chem Int Ed Engl. 2015 Aug 17;54(34):10030-4. doi: 10.1002/anie.201502868. Epub 2015 Jul 1.

Chemical Evolution of a Bacterial Proteome.

Author information

1
Institut für Chemie, Technische Universität 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 Universität 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).
7
Institut für Chemie, Technische Universität Berlin, Müller-Breslau-Strasse 10, 10623 Berlin (Germany). nediljko.budisa@tu-berlin.de.

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-(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.

KEYWORDS:

Escherichia coli; continuous evolution; genetic code translation; synthetic biology; tryptophan analogues

PMID:
26136259
PMCID:
PMC4782924
DOI:
10.1002/anie.201502868
[Indexed for MEDLINE]
Free PMC Article
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