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Issue 19, 2020
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Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis

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Abstract

Inherent promiscuity of bacterial translation is demonstrated by mass spectrometric quantification of the translational incorporation of ring-substituted phenylalanines and tyrosines bearing fluoro-, hydroxyl-, methyl-, chloro- and nitro-groups in an E. coli-derived cell-free system. Competitive studies using the cell-free system show that the aminoacyl-tRNA synthetases (aaRS) have at least two orders of magnitude higher specificity for the native substrate over these structural analogues, which correlates with studies on the purified synthetase.

Graphical abstract: Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis

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Supplementary files

Article information


Submitted
21 Jan 2020
Accepted
09 Mar 2020
First published
18 Mar 2020

This article is Open Access

RSC Adv., 2020,10, 11013-11023
Article type
Paper

Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis

Z. Wang and H. Matthews, RSC Adv., 2020, 10, 11013
DOI: 10.1039/D0RA00655F

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