Transmembrane but not soluble helices fold inside the ribosome tunnel

Manuel Bañó-Polo, Carlos Baeza-Delgado, Silvia Tamborero, Anthony Hazel, Brayan Grau, IngMarie Nilsson, Paul Whitley, James C. Gumbart, Gunnar Heijne and Ismael Mingarro ()
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Manuel Bañó-Polo: Universitat de València
Carlos Baeza-Delgado: Universitat de València
Silvia Tamborero: Universitat de València
Anthony Hazel: Georgia Institute of Technology
Brayan Grau: Universitat de València
IngMarie Nilsson: Stockholm University
Paul Whitley: University of Bath
James C. Gumbart: Georgia Institute of Technology
Gunnar Heijne: Stockholm University
Ismael Mingarro: Universitat de València

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-07554-7

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