Reassembling green fluorescent protein for in vitro evaluation of trans-translation

In order to discover new antibiotics with improved activity and selectivity, we created a reliable in vitro reporter system to detect trans-translation activity, the main mechanism for recycling ribosomes stalled on problematic messenger RNA (mRNA) in bacteria. This system is based on an engineered...

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Autores principales: Guyomar, Charlotte, Thépaut, Marion, Nonin-Lecomte, Sylvie, Méreau, Agnès, Goude, Renan, Gillet, Reynald
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Methods Online
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7038980/
https://www.ncbi.nlm.nih.gov/pubmed/31919515
http://dx.doi.org/10.1093/nar/gkz1204
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author Guyomar, Charlotte
Thépaut, Marion
Nonin-Lecomte, Sylvie
Méreau, Agnès
Goude, Renan
Gillet, Reynald
author_facet Guyomar, Charlotte
Thépaut, Marion
Nonin-Lecomte, Sylvie
Méreau, Agnès
Goude, Renan
Gillet, Reynald
author_sort Guyomar, Charlotte
collection PubMed
description In order to discover new antibiotics with improved activity and selectivity, we created a reliable in vitro reporter system to detect trans-translation activity, the main mechanism for recycling ribosomes stalled on problematic messenger RNA (mRNA) in bacteria. This system is based on an engineered tmRNA variant that reassembles the green fluorescent protein (GFP) when trans-translation is active. Our system is adapted for high-throughput screening of chemical compounds by fluorescence.
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spelling pubmed-70389802020-03-02 Reassembling green fluorescent protein for in vitro evaluation of trans-translation Guyomar, Charlotte Thépaut, Marion Nonin-Lecomte, Sylvie Méreau, Agnès Goude, Renan Gillet, Reynald Nucleic Acids Res Methods Online In order to discover new antibiotics with improved activity and selectivity, we created a reliable in vitro reporter system to detect trans-translation activity, the main mechanism for recycling ribosomes stalled on problematic messenger RNA (mRNA) in bacteria. This system is based on an engineered tmRNA variant that reassembles the green fluorescent protein (GFP) when trans-translation is active. Our system is adapted for high-throughput screening of chemical compounds by fluorescence. Oxford University Press 2020-02-28 2020-01-10 /pmc/articles/PMC7038980/ /pubmed/31919515 http://dx.doi.org/10.1093/nar/gkz1204 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Methods Online
Guyomar, Charlotte
Thépaut, Marion
Nonin-Lecomte, Sylvie
Méreau, Agnès
Goude, Renan
Gillet, Reynald
Reassembling green fluorescent protein for in vitro evaluation of trans-translation
title Reassembling green fluorescent protein for in vitro evaluation of trans-translation
title_full Reassembling green fluorescent protein for in vitro evaluation of trans-translation
title_fullStr Reassembling green fluorescent protein for in vitro evaluation of trans-translation
title_full_unstemmed Reassembling green fluorescent protein for in vitro evaluation of trans-translation
title_short Reassembling green fluorescent protein for in vitro evaluation of trans-translation
title_sort reassembling green fluorescent protein for in vitro evaluation of trans-translation
topic Methods Online
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7038980/
https://www.ncbi.nlm.nih.gov/pubmed/31919515
http://dx.doi.org/10.1093/nar/gkz1204
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