Advances in the mechanism and understanding of site-selective noncanonical amino acid incorporation

Antonczak, Alicja K., Morris, Josephine Lydia and Tippmann, Eric Michael 2011. Advances in the mechanism and understanding of site-selective noncanonical amino acid incorporation. Current Opinion in Structural Biology 21 (4) , pp. 481-487. 10.1016/j.sbi.2011.04.004

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Abstract

There are many approaches to introduce non-native functionality into proteins either translationally or post-translationally. When a noncanonical amino acid (NAA) is incorporated translationally, the host organism's existing translational machinery is relied upon to insert the amino acid by the same well-established mechanisms used by the host to achieve high fidelity insertion of its canonical amino acids. Research into the in vivo incorporation of NAAs has typically concentrated on evolving or engineering aminoacyl tRNA synthetases (aaRSs); however, new studies have increasingly focused on other members of the translational apparatus, for example entire ribosomes, in attempts to increase the fidelity and efficiency of incorporation of ever more structurally diverse NAAs. As the biochemical methods of NAA systems increase in complexity, it is informative to ask whether the ‘rules’ for canonical translation (i.e. aaRSs, tRNA, ribosomes, elongation factors, amino acid uptake, and metabolism) hold for NAA systems, or whether new rules are warranted. Here, recent advances in introducing novel chemical functionality into proteins are highlighted.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Subjects:	Q Science > QD Chemistry
Publisher:	Elsevier
ISSN:	0959-440x
Last Modified:	05 Jan 2018 21:15
URI:	https://orca.cardiff.ac.uk/id/eprint/16216

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