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Cotranslational folding of spectrin domains via partially structured states.

Abstract：

: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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Nilsson OB,Nickson AA,Hollins JJ,Wickles S,Steward A,Beckmann R,von Heijne G,Clarke J

doi

10.1038/nsmb.3355

subject

Has Abstract

pub_date

2017-03-01 00:00:00

pages

221-225

issue

3

eissn

1545-9993

issn

1545-9985

pii

nsmb.3355

journal_volume

24

pub_type

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