Waudby, CA;
Dobson, CM;
Christodoulou, J;
(2019)
Nature and Regulation of Protein Folding on the Ribosome.
Trends in Biochemical Sciences
, 44
(11)
pp. 914-926.
10.1016/j.tibs.2019.06.008.
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Abstract
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.
| Type: | Article |
|---|---|
| Title: | Nature and Regulation of Protein Folding on the Ribosome |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.tibs.2019.06.008 |
| Publisher version: | https://doi.org/10.1016/j.tibs.2019.06.008 |
| Language: | English |
| Additional information: | © 2019 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| Keywords: | co-translational folding, free energy landscape, molecular chaperones, protein synthesis, translation kinetics |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10078146 |
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