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

Cabrita, Lisa D. and Cassaignau, Anaïs M.E. and Launay, Hélène M.M. and Waudby, Christopher A. and Wlodarski, Tomasz and Camilloni, C. and Karyadi, Maria-Evangelia and Robertson, Amy L. and Wang, Xiaolin and Wentink, Anne S. and Goodsell, Luke S. and Woolhead, C.A. and Vendruscolo, M. and Dobson, C.M. and Christodoulou, John (2016) A structural ensemble of a ribosome–nascent chain complex during cotranslational protein folding. Nature Structural & Molecular Biology 23 (4), pp. 278-285. ISSN 1545-9993.

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Official URL: http://doi.org/10.1038/nsmb.3182

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.

Metadata

Item Type:	Article
School:	Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
Research Centres and Institutes:	Structural Molecular Biology, Institute of (ISMB)
Depositing User:	Administrator
Date Deposited:	04 Mar 2016 09:59
Last Modified:	02 Aug 2023 17:22
URI:	https://eprints.bbk.ac.uk/id/eprint/14594

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