Reassigning Sense Codon AGA to Encode Noncanonical Amino Acids inEscherichia coli

ChemBioChem ◽  
2016 ◽  
Vol 17 (23) ◽  
pp. 2234-2239 ◽  
Author(s):  
Yiyan Wang ◽  
Meng-Lin Tsao
Keyword(s):  
Amino Acids ◽  
Inescherichia Coli ◽  
Noncanonical Amino Acids ◽  
Sense Codon

A Facile System for Genetic Incorporation of Two Different Noncanonical Amino Acids into One Protein inEscherichia coli

2010 ◽  
Vol 49 (18) ◽  
pp. 3211-3214 ◽  
Author(s):  
Wei Wan ◽  
Ying Huang ◽  
Zhiyong Wang ◽  
William K. Russell ◽  
Pei-Jing Pai ◽  
...  
Keyword(s):  
Amino Acids ◽  
Inescherichia Coli ◽  
Noncanonical Amino Acids ◽  
Genetic Incorporation

A Facile System for Genetic Incorporation of Two Different Noncanonical Amino Acids into One Protein inEscherichia coli

2010 ◽  
Vol 122 (18) ◽  
pp. 3279-3282 ◽  
Author(s):  
Wei Wan ◽  
Ying Huang ◽  
Zhiyong Wang ◽  
William K. Russell ◽  
Pei-Jing Pai ◽  
...  
Keyword(s):  
Amino Acids ◽  
Inescherichia Coli ◽  
Noncanonical Amino Acids ◽  
Genetic Incorporation

Noncanonical Amino Acids for Hypoxia-Responsive Peptide Self-Assembly and Fluorescence

2021 ◽  
Author(s):  
Binbin Hu ◽  
Na Song ◽  
Yawei Cao ◽  
Mingming Li ◽  
Xin Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Noncanonical Amino Acids

scholarly journals Sense codon reassignment enables viral resistance and encoded polymer synthesis

Science ◽  
2021 ◽  
Vol 372 (6546) ◽  
pp. 1057-1062
Author(s):  
Wesley E. Robertson ◽  
Louise F. H. Funke ◽  
Daniel de la Torre ◽  
Julius Fredens ◽  
Thomas S. Elliott ◽  
...  
Keyword(s):  
Stop Codon ◽  
Synonymous Codon ◽  
Viral Resistance ◽  
Release Factor ◽  
Codon Reassignment ◽  
Efficient Synthesis ◽  
Noncanonical Amino Acids ◽  
Laboratory Evolution ◽  
Transfer Rnas ◽  
Sense Codon

It is widely hypothesized that removing cellular transfer RNAs (tRNAs)—making their cognate codons unreadable—might create a genetic firewall to viral infection and enable sense codon reassignment. However, it has been impossible to test these hypotheses. In this work, following synonymous codon compression and laboratory evolution in Escherichia coli, we deleted the tRNAs and release factor 1, which normally decode two sense codons and a stop codon; the resulting cells could not read the canonical genetic code and were completely resistant to a cocktail of viruses. We reassigned these codons to enable the efficient synthesis of proteins containing three distinct noncanonical amino acids. Notably, we demonstrate the facile reprogramming of our cells for the encoded translation of diverse noncanonical heteropolymers and macrocycles.

scholarly journals Genetic Encoding of Three Distinct Noncanonical Amino Acids Using Reprogrammed Initiator and Nonsense Codons

2021 ◽  
Vol 16 (4) ◽  
pp. 766-774
Author(s):  
Jeffery M. Tharp ◽  
Oscar Vargas-Rodriguez ◽  
Alanna Schepartz ◽  
Dieter Söll
Keyword(s):  
Amino Acids ◽  
Noncanonical Amino Acids ◽  
Genetic Encoding ◽  
Nonsense Codons

scholarly journals Reassignment of a rare sense codon to a non-canonical amino acid inEscherichia coli

2015 ◽  
Vol 43 (16) ◽  
pp. 8111-8122 ◽  
Author(s):  
Takahito Mukai ◽  
Atsushi Yamaguchi ◽  
Kazumasa Ohtake ◽  
Mihoko Takahashi ◽  
Akiko Hayashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Inescherichia Coli ◽  
Canonical Amino Acid ◽  
Sense Codon

scholarly journals A Genetically Encoded Picolyl Azide for Improved Live Cell Copper Click Labeling

2021 ◽  
Vol 9 ◽  
Author(s):  
Birthe Meineke ◽  
Johannes Heimgärtner ◽  
Alexander J. Craig ◽  
Michael Landreh ◽  
Lindon W. K. Moodie ◽  
...  
Keyword(s):  
Amino Acids ◽  
Mammalian Cells ◽  
Stop Codon ◽  
Bioorthogonal Chemistry ◽  
Bioorthogonal Reaction ◽  
Noncanonical Amino Acids ◽  
Selective Reactivity ◽  
Direct Incorporation ◽  
Chelating Groups ◽  
Amber Suppression

Bioorthogonal chemistry allows rapid and highly selective reactivity in biological environments. The copper-catalyzed azide–alkyne cycloaddition (CuAAC) is a classic bioorthogonal reaction routinely used to modify azides or alkynes that have been introduced into biomolecules. Amber suppression is an efficient method for incorporating such chemical handles into proteins on the ribosome, in which noncanonical amino acids (ncAAs) are site specifically introduced into the polypeptide in response to an amber (UAG) stop codon. A variety of ncAA structures containing azides or alkynes have been proven useful for performing CuAAC chemistry on proteins. To improve CuAAC efficiency, biologically incorporated alkyne groups can be reacted with azide substrates that contain copper-chelating groups. However, the direct incorporation of copper-chelating azides into proteins has not been explored. To remedy this, we prepared the ncAA paz-lysine (PazK), which contains a picolyl azide motif. We show that PazK is efficiently incorporated into proteins by amber suppression in mammalian cells. Furthermore, PazK-labeled proteins show improved reactivity with alkyne reagents in CuAAC.

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