Chemical Evolution of a Bacterial Proteome. Issue 34 (1st July 2015)

• Record Type: Journal Article
• Authors: Hoesl, Michael Georg; Oehm, Stefan; Durkin, Patrick; Darmon, Elise; Peil, Lauri; Aerni, Hans‐Rudolf; Rappsilber, Juri; Rinehart, Jesse; Leach, David; Söll, Dieter; Budisa, Nediljko
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 34(2015)
• Page Start: 10030
• Page End: 10034
• Publication Date: 2015-07-01
• Subjects: continuous evolution -- Escherichia coli -- genetic code translation -- synthetic biology -- tryptophan analogues; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201502868
• Languages: English
• ISSNs: 1433-7851

Abstract

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. Abstract : Towards synthetic bacteria : An evolution experiment in synthetic medium led to quantitative substitution of tryptophan with L ‐β‐(thieno[3, 2‐ b ]pyrrolyl)alanine in response to 20 899 TGG codons in bacterium Escherichia coli W3110. The evolved bacteria showed robust growth in the complete absence of Trp without significant adverse effects on the cellular survival.