Issue 19, 2020

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

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

Supplementary files

Article information

Article type
Paper
Submitted
21 jan. 2020
Accepted
09 mar. 2020
First published
18 mar. 2020
This article is Open Access
Creative Commons BY license

RSC Adv., 2020,10, 11013-11023

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

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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