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Transmembrane but not soluble helices fold inside the ribosome tunnel
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Number of Authors: 102018 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 9, article id 5246Article in journal (Refereed) Published
Abstract [en]

Integral membrane proteins are assembled into the ER membrane via a continuous ribosome-translocon channel. The hydrophobicity and thickness of the core of the membrane bilayer leads to the expectation that transmembrane (TM) segments minimize the cost of harbouring polar polypeptide backbones by adopting a regular pattern of hydrogen bonds to form a-helices before integration. Co-translational folding of nascent chains into an a-helical conformation in the ribosomal tunnel has been demonstrated previously, but the features governing this folding are not well understood. In particular, little is known about what features influence the propensity to acquire a-helical structure in the ribosome. Using in vitro translation of truncated nascent chains trapped within the ribosome tunnel and molecular dynamics simulations, we show that folding in the ribosome is attained for TM helices but not for soluble helices, presumably facilitating SRP (signal recognition particle) recognition and/or a favourable conformation for membrane integration upon translocon entry.

Place, publisher, year, edition, pages
2018. Vol. 9, article id 5246
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Biological Sciences
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URN: urn:nbn:se:su:diva-163699DOI: 10.1038/s41467-018-07554-7ISI: 000452633200005PubMedID: 30531789OAI: oai:DiVA.org:su-163699DiVA, id: diva2:1280257
Available from: 2019-01-18 Created: 2019-01-18 Last updated: 2019-01-18Bibliographically approved

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Nilsson, IngMarievon Heijne, Gunnar
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Department of Biochemistry and Biophysics
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