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Nature and Regulation of Protein Folding on the Ribosome

Co-translational protein folding is an essential process by which cells ensure the safe and efficient production and assembly of new proteins in their functional native states following biosynthesis on the ribosome. In this review, we describe recent progress in probing the changes during protein sy...

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Detalles Bibliográficos
Autores principales: Waudby, Christopher A., Dobson, Christopher M., Christodoulou, John
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Trends Journals 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7471843/
https://www.ncbi.nlm.nih.gov/pubmed/31301980
http://dx.doi.org/10.1016/j.tibs.2019.06.008
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author Waudby, Christopher A.
Dobson, Christopher M.
Christodoulou, John
author_facet Waudby, Christopher A.
Dobson, Christopher M.
Christodoulou, John
author_sort Waudby, Christopher A.
collection PubMed
description Co-translational protein folding is an essential process by which cells ensure the safe and efficient production and assembly of new proteins in their functional native states following biosynthesis on the ribosome. In this review, we describe recent progress in probing the changes during protein synthesis of the free energy landscapes that underlie co-translational folding and discuss the critical coupling between these landscapes and the rate of translation that ultimately determines the success or otherwise of the folding process. Recent developments have revealed a variety of mechanisms by which both folding and translation can be modulated or regulated, and we discuss how these effects are utilised by the cell to optimise the outcome of protein biosynthesis.
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spelling pubmed-74718432020-09-11 Nature and Regulation of Protein Folding on the Ribosome Waudby, Christopher A. Dobson, Christopher M. Christodoulou, John Trends Biochem Sci Article Co-translational protein folding is an essential process by which cells ensure the safe and efficient production and assembly of new proteins in their functional native states following biosynthesis on the ribosome. In this review, we describe recent progress in probing the changes during protein synthesis of the free energy landscapes that underlie co-translational folding and discuss the critical coupling between these landscapes and the rate of translation that ultimately determines the success or otherwise of the folding process. Recent developments have revealed a variety of mechanisms by which both folding and translation can be modulated or regulated, and we discuss how these effects are utilised by the cell to optimise the outcome of protein biosynthesis. Elsevier Trends Journals 2019-11 /pmc/articles/PMC7471843/ /pubmed/31301980 http://dx.doi.org/10.1016/j.tibs.2019.06.008 Text en © 2019 The Author(s) http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Waudby, Christopher A.
Dobson, Christopher M.
Christodoulou, John
Nature and Regulation of Protein Folding on the Ribosome
title Nature and Regulation of Protein Folding on the Ribosome
title_full Nature and Regulation of Protein Folding on the Ribosome
title_fullStr Nature and Regulation of Protein Folding on the Ribosome
title_full_unstemmed Nature and Regulation of Protein Folding on the Ribosome
title_short Nature and Regulation of Protein Folding on the Ribosome
title_sort nature and regulation of protein folding on the ribosome
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7471843/
https://www.ncbi.nlm.nih.gov/pubmed/31301980
http://dx.doi.org/10.1016/j.tibs.2019.06.008
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