Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 4, Pages 278-285Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3182
Keywords
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Funding
- Wellcome Trust [094425/Z/10/Z, 097806/Z/11/Z]
- Alpha-1 Foundation grant
- Biotechnology and Biochemical Sciences Research Council [BBG0156511]
- National Health and Medical Research Council (Australia)
- European Molecular Biology Organization
- Wellcome Trust [097806/Z/11/Z] Funding Source: Wellcome Trust
- BBSRC [BB/G015651/1] Funding Source: UKRI
- MRC [MC_U117533887] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G015651/1] Funding Source: researchfish
- Medical Research Council [MC_U117533887] Funding Source: researchfish
- The Francis Crick Institute [10029] Funding Source: researchfish
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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.
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