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Translation of target gene transcripts in  Escherichia coli  harboring UAG amber stop codons can be switched on by the amber-codon-specific incorporation of an exogenously supplied unnatural amino acid, 3-iodo- L -tyrosine. Here, we report that this translational switch can control the translational efficiency at any intermediate magnitude by adjustment of the 3-iodo- L -tyrosine concentration in the medium, as a tunable translational controller. The translational efficiency of a target gene reached maximum levels with 10 −5  M 3-iodo- L -tyrosine, and intermediate levels were observed with suboptimal concentrations (approximately spanning a 2-log 10  concentration range, 10 −7 –10 −5  M). Such intermediate-level expression was also confirmed in individual bacteria.

Tunable translational control using site-specific unnatural amino acid incorporation inEscherichia coli