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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.

SUBMITTER: Wang Z

PROVIDER: S-EPMC9050441 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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

Wang Zhongqiang Z Matthews Hayden H

RSC advances 20200318 19

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 <i>E. coli</i>-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 ...[more]

PMID: 35495348

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