scholarly journals Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques

1993 ◽  
Vol 2 (3) ◽  
pp. 395-403 ◽  
Author(s):  
R. Wynn ◽  
F. M. Richards
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Chemical Modification ◽  
Unnatural Amino Acid ◽  
Combined Mutagenesis

scholarly journals A Versatile Platform for Single- and Multiple-Unnatural Amino Acid Mutagenesis in Escherichia coli

Biochemistry ◽  
2013 ◽  
Vol 52 (10) ◽  
pp. 1828-1837 ◽  
Author(s):  
Abhishek Chatterjee ◽  
Sophie B. Sun ◽  
Jennifer L. Furman ◽  
Han Xiao ◽  
Peter G. Schultz
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Unnatural Amino Acid Mutagenesis ◽  
Amino Acid Mutagenesis

scholarly journals Tunable translational control using site-specific unnatural amino acid incorporation in Escherichia coli

2015 ◽  
Author(s):  
Yusuke Kato
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Translational Control ◽  
Target Gene ◽  
Unnatural Amino Acid ◽  
Translational Efficiency ◽  
Amino Acid Incorporation ◽  
Amber Codon ◽  
Gene Transcripts ◽  
Tyrosine Concentration

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-log10 concentration range, 10-7 to 10-5 M). Such intermediate-level expression was also confirmed in individual bacteria.

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