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Transmembrane but not soluble helices fold inside the ribosome tunnel

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Transmembrane but not soluble helices fold inside the ribosome tunnel

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dc.contributor.author Bañó Polo, Manuel
dc.contributor.author Baeza Delgado, Carlos
dc.contributor.author Tamborero Capilla, Silvia
dc.contributor.author Hazel, Anthony
dc.contributor.author Grau, Brayan
dc.contributor.author Nilsson, IngMarie
dc.contributor.author Whitley, Paul
dc.contributor.author Gumbart, James C.
dc.contributor.author Heijne, Gunnar von
dc.contributor.author Mingarro Muñoz, Ismael
dc.date.accessioned 2019-05-07T13:10:27Z
dc.date.available 2019-05-07T13:10:27Z
dc.date.issued 2018
dc.identifier.citation Bañó Polo, Manuel Baeza Delgado, Carlos Tamborero Capilla, Silvia Hazel, Anthony Grau, Brayan Nilsson, IngMarie Whitley, Paul Gumbart, James C. Heijne, Gunnar von Mingarro Muñoz, Ismael 2018 Transmembrane but not soluble helices fold inside the ribosome tunnel Nature Communications 9 5246 1 9
dc.identifier.uri http://hdl.handle.net/10550/70100
dc.description.abstract 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 α-helices before integration. Co-translational folding of nascent chains into an α-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 α-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.
dc.language.iso eng
dc.relation.ispartof Nature Communications, 2018, vol. 9, num. 5246, p. 1-9
dc.subject Proteïnes de membrana
dc.subject Ribosomes
dc.title Transmembrane but not soluble helices fold inside the ribosome tunnel
dc.type journal article es_ES
dc.date.updated 2019-05-07T13:10:27Z
dc.identifier.doi 10.1038/s41467-018-07554-7
dc.identifier.idgrec 129598
dc.rights.accessRights open access es_ES

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