Structural highlights
Publication Abstract from PubMed
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.
Cotranslational folding of spectrin domains via partially structured states.,Nilsson OB, Nickson AA, Hollins JJ, Wickles S, Steward A, Beckmann R, von Heijne G, Clarke J Nat Struct Mol Biol. 2017 Jan 23. doi: 10.1038/nsmb.3355. PMID:28112730[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nilsson OB, Nickson AA, Hollins JJ, Wickles S, Steward A, Beckmann R, von Heijne G, Clarke J. Cotranslational folding of spectrin domains via partially structured states. Nat Struct Mol Biol. 2017 Jan 23. doi: 10.1038/nsmb.3355. PMID:28112730 doi:http://dx.doi.org/10.1038/nsmb.3355
