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

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 stu...

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Autores principales: Wang, Zhongqiang, Matthews, Hayden
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9050441/
https://www.ncbi.nlm.nih.gov/pubmed/35495348
http://dx.doi.org/10.1039/d0ra00655f
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author Wang, Zhongqiang
Matthews, Hayden
author_facet Wang, Zhongqiang
Matthews, Hayden
author_sort Wang, Zhongqiang
collection PubMed
description 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.
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spelling pubmed-90504412022-04-29 Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis Wang, Zhongqiang Matthews, Hayden RSC Adv Chemistry 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. The Royal Society of Chemistry 2020-03-18 /pmc/articles/PMC9050441/ /pubmed/35495348 http://dx.doi.org/10.1039/d0ra00655f Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Wang, Zhongqiang
Matthews, Hayden
Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
title Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
title_full Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
title_fullStr Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
title_full_unstemmed Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
title_short Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
title_sort translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9050441/
https://www.ncbi.nlm.nih.gov/pubmed/35495348
http://dx.doi.org/10.1039/d0ra00655f
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