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Cotranslational folding of spectrin domains via partially structured states
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2017 (English)In: Nature Structural & Molecular Biology, ISSN 1545-9993, E-ISSN 1545-9985, Vol. 24, no 3, 221-225 p.Article in journal (Refereed) Published
Abstract [en]

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 α-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.

Place, publisher, year, edition, pages
2017. Vol. 24, no 3, 221-225 p.
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Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-140964DOI: 10.1038/nsmb.3355ISI: 000395826000005PubMedID: 28112730OAI: oai:DiVA.org:su-140964DiVA: diva2:1084544
Available from: 2017-03-25 Created: 2017-03-25 Last updated: 2017-04-03Bibliographically approved

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Nilsson, Ola B.von Heijne, Gunnar
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