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A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding

Cabrita, LD; Cassaignau, AM; Launay, HM; Waudby, CA; Wlodarski, T; Camilloni, C; Karyadi, ME; ... Christodoulou, J; + view all (2016) A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding. Nature Structural and Molecular Biology , 23 (4) pp. 278-285. 10.1038/nsmb.3182. Green open access

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Abstract

Although detailed pictures of ribosome structures are emerging, little is known about the structural and cotranslational folding properties of nascent polypeptide chains at the atomic level. Here we used solution-state NMR spectroscopy to define a structural ensemble of a ribosome-nascent chain complex (RNC) formed during protein biosynthesis in Escherichia coli, in which a pair of immunoglobulin-like domains adopts a folded N-terminal domain (FLN5) and a disordered but compact C-terminal domain (FLN6). To study how FLN5 acquires its native structure cotranslationally, we progressively shortened the RNC constructs. We found that the ribosome modulates the folding process, because the complete sequence of FLN5 emerged well beyond the tunnel before acquiring native structure, whereas FLN5 in isolation folded spontaneously, even when truncated. This finding suggests that regulating structure acquisition during biosynthesis can reduce the probability of misfolding, particularly of homologous domains.

Type: Article
Title: A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/nsmb.3182
Publisher version: http://dx.doi.org/10.1038/nsmb.3182
Language: English
Additional information: Copyright © 2016 Nature America, Inc. All rights reserved. This is the accepted manuscript version of the article published in Nature Structural and Molecular Biology; the final published version is available at http://dx.doi.org/10.1038/nsmb.3182
Keywords: Protein folding, Ribosome, Solution-state NMR
UCL classification: UCL > Provost and Vice Provost Offices
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: http://discovery.ucl.ac.uk/id/eprint/1481139
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