Chemical Evolution of a Bacterial Proteome.
Chemical Evolution of a Bacterial Proteome.
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DOI:
10.1002/anie.201502868
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发表时间:
2015-08-17
期刊:
影响因子:
--
通讯作者:
Budisa N
中科院分区:
文献类型:
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作者:
Hoesl MG;Oehm S;Durkin P;Darmon E;Peil L;Aerni HR;Rappsilber J;Rinehart J;Leach D;Söll D;Budisa N
We have changed the amino acid set of the genetic code of Escherichia coli by evolving cultures capable of growing on the synthetic non-canonical 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 are capable of 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. Towards synthetic bacteria: An evolution experiment in synthetic medium led to quantitative Tryptophan to L-β-(thieno[3,2-b]pyrrolyl)-alanine substitution in response to 20,899 TGG codons in bacterium Escherichia coli W3110. The evolved bacteria were capable of robust growth in the complete absence of Trp without significant adverse effects on the cellular survival.