Orthogonal Protein Translation Using Pyrrolysyl-tRNA Synthetases for Single- and Multiple-Noncanonical Amino Acid Mutagenesis

descriptionPublicationkeyboard_double_arrow_right Part of book or chapter of book , Article 01 Jan 2016 English Publisher:Springer International Publishing

Authors: Tobias, Baumann; Matthias, Exner; Nediljko, Budisa;

doi: 10.1007/10_2016_37

pmid: 27783132

Orthogonal Protein Translation Using Pyrrolysyl-tRNA Synthetases for Single- and Multiple-Noncanonical Amino Acid Mutagenesis

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Abstract

To date, the two systems most extensively used for noncanonical amino acid (ncAA) incorporation via orthogonal translation are based on the Methanococcus jannaschii TyrRS/tRNA CUATyr and the Methanosarcina barkeri/Methanosarcina mazei PylRS/tRNA CUAPyl pairs. Here, we summarize the development and usage of the pyrrolysine-based system for orthogonal translation, a process that allows for the recombinant production of site-specifically labeled proteins and peptides. Via stop codon suppression in Escherichia coli and mammalian cells, genetically encoded biomolecules can be equipped with a great diversity of chemical functionalities including click chemistry handles, post-translational modifications, and photocaged sidechains.

Related Organizations

Technical University of Berlin
Germany
Technical University of Berlin
Germany

Keywords

Amino Acyl-tRNA Synthetases, Suppression, Genetic, Bacterial Proteins, Mutagenesis, Methanococcus, Protein Biosynthesis, Methanosarcina, Codon, Terminator, Escherichia coli

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