Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 138, Issue 16, Pages 5194-5197Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b01023
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- NSF [DGE-1122492]
- NIGMS [GM22854]
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It has recently been reported that ribosomes from erythromycin-resistant Escherichia coli strains, when isolated in S30 extracts and incubated with chemically mis-acylated tRNA, can incorporate certain beta-amino acids into full length DHFR in vitro. Here we report that wild-type E. coli EF-Tu and phenylalanyl-tRNA synthetase collaborate with these mutant ribosomes and others to incorporate beta(3)-Phe analogs into full length DHFR in vivo. E. coli harboring the most active mutant ribosomes are robust, with a doubling time only 14% longer than wild-type. These results reveal the unexpected tolerance of E. coli and its translation machinery to the beta(3)-amino acid backbone and should embolden in vivo selections for orthogonal translational machinery components that, incorporate diverse beta-amino acids into proteins and peptides. E. coli harboring mutant ribosomes may possess the capacity to incorporate many non-natural, non alpha-amino acids into proteins and other sequence programmed polymeric materials.
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