Engineering Heterodimeric Kinesins through Genetic Incorporation of Noncanonical Amino Acids

2018 ◽  
Vol 13 (8) ◽  
pp. 2229-2236
Author(s):  
Andrew R. Popchock ◽  
Subhashis Jana ◽  
Ryan A. Mehl ◽  
Weihong Qiu
Keyword(s):  
Amino Acids ◽  
Noncanonical Amino Acids ◽  
Genetic Incorporation

scholarly journals Genetic Incorporation of Noncanonical Amino Acids Using Two Mutually Orthogonal Quadruplet Codons

2019 ◽  
Vol 8 (5) ◽  
pp. 1168-1174 ◽  
Author(s):  
Erome Daniel Hankore ◽  
Linyi Zhang ◽  
Yan Chen ◽  
Kun Liu ◽  
Wei Niu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Noncanonical Amino Acids ◽  
Genetic Incorporation

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

scholarly journals Plasticity and Constraints of tRNA Aminoacylation Define Directed Evolution of Aminoacyl-tRNA Synthetases

2019 ◽  
Vol 20 (9) ◽  
pp. 2294 ◽  
Author(s):  
Ana Crnković ◽  
Oscar Vargas-Rodriguez ◽  
Dieter Söll
Keyword(s):  
Amino Acids ◽  
Directed Evolution ◽  
Active Site ◽  
Nonsense Suppression ◽  
Natural Amino Acid ◽  
Noncanonical Amino Acids ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Genetic Incorporation

Genetic incorporation of noncanonical amino acids (ncAAs) has become a powerful tool to enhance existing functions or introduce new ones into proteins through expanded chemistry. This technology relies on the process of nonsense suppression, which is made possible by directing aminoacyl-tRNA synthetases (aaRSs) to attach an ncAA onto a cognate suppressor tRNA. However, different mechanisms govern aaRS specificity toward its natural amino acid (AA) substrate and hinder the engineering of aaRSs for applications beyond the incorporation of a single l-α-AA. Directed evolution of aaRSs therefore faces two interlinked challenges: the removal of the affinity for cognate AA and improvement of ncAA acylation. Here we review aspects of AA recognition that directly influence the feasibility and success of aaRS engineering toward d- and β-AAs incorporation into proteins in vivo. Emerging directed evolution methods are described and evaluated on the basis of aaRS active site plasticity and its inherent constraints.

A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli

2010 ◽  
Vol 6 (4) ◽  
pp. 683 ◽  
Author(s):  
Ying Huang ◽  
William K. Russell ◽  
Wei Wan ◽  
Pei-Jing Pai ◽  
David H. Russell ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Convenient Method ◽  
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 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

Two site genetic incorporation of varying length polyethylene glycol into the backbone of one peptide

2015 ◽  
Vol 51 (76) ◽  
pp. 14385-14388 ◽  
Author(s):  
Qingmin Zang ◽  
Seiichi Tada ◽  
Takanori Uzawa ◽  
Daisuke Kiga ◽  
Masayuki Yamamura ◽  
...  
Keyword(s):  
Amino Acids ◽  
Polyethylene Glycol ◽  
Varying Length ◽  
Genetic Incorporation

Polyethylene glycol (PEG) of different lengths was genetically incorporated into the backbone of a polypeptide using stop-anticodon and frameshift anticodon-containing tRNAs, which were acylated with PEG-containing amino acids.

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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