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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2020
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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. |
format | Online Article Text |
id | pubmed-9050441 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT wangzhongqiang translationalincorporationofmodifiedphenylalaninesandtyrosinesduringcellfreeproteinsynthesis AT matthewshayden translationalincorporationofmodifiedphenylalaninesandtyrosinesduringcellfreeproteinsynthesis |