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Cotranslational folding of spectrin domains via partially structured states

Nilsson, Ola B. (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Nickson, Adrian A. (author)
Hollins, Jeffrey J. (author)
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Wickles, Stephan (author)
Steward, Annette (author)
Beckmann, Roland (author)
von Heijne, Gunnar (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
Clarke, Jane (author)
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 (creator_code:org_t)
2017-01-23
2017
English.
In: Nature Structural & Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 24:3, s. 221-225
  • Journal article (peer-reviewed)
Abstract Subject headings
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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 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

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