Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 24, Issue 3, Pages 221-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3355
Keywords
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Funding
- Swedish Cancer Foundation
- Swedish Research Council
- Knut and Alice Wallenberg Foundation
- Wellcome Trust [WT095195]
- European Research Council [ERC-2008-AdG 232648]
- MRC [MC_U105485808] Funding Source: UKRI
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How do the key features of protein folding, elucidated from studies on native, isolated proteins, manifest in cotranslational folding on the ribosome? Using a well-characterized family of homologous alpha-helical proteins with a range of biophysical properties, we show that spectrin domains can fold vectorially on the ribosome and may do so via a pathway different from that of the isolated domain. We use cryo-EM to reveal a folded or partially folded structure, formed in the vestibule of the ribosome. Our results reveal that it is not possible to predict which domains will fold within the ribosome on the basis of the folding behavior of isolated domains; instead, we propose that a complex balance of the rate of folding, the rate of translation and the lifetime of folded or partly folded states will determine whether folding occurs cotranslationally on actively translating ribosomes.
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