Molecular code for transmembrane-helix recognition by the Sec61 translocon

Tara Hessa, Nadja M. Meindl-Beinker, Andreas Bernsel, Hyun Kim, Yoko Sato, Mirjam Lerch-Bader, IngMarie Nilsson, Stephen H. White and Gunnar von Heijne ()
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Tara Hessa: Center for Biomembrane Research, Stockholm University
Nadja M. Meindl-Beinker: Center for Biomembrane Research, Stockholm University
Andreas Bernsel: Stockholm Bioinformatics Center, AlbaNova, Stockholm University
Hyun Kim: Center for Biomembrane Research, Stockholm University
Yoko Sato: Center for Biomembrane Research, Stockholm University
Mirjam Lerch-Bader: Center for Biomembrane Research, Stockholm University
IngMarie Nilsson: Center for Biomembrane Research, Stockholm University
Stephen H. White: University of California at Irvine, Irvine, California 92697-4560, USA
Gunnar von Heijne: Center for Biomembrane Research, Stockholm University

Nature, 2007, vol. 450, issue 7172, 1026-1030

Abstract: Abstract Transmembrane α-helices in integral membrane proteins are recognized co-translationally and inserted into the membrane of the endoplasmic reticulum by the Sec61 translocon. A full quantitative description of this phenomenon, linking amino acid sequence to membrane insertion efficiency, is still lacking. Here, using in vitro translation of a model protein in the presence of dog pancreas rough microsomes to analyse a large number of systematically designed hydrophobic segments, we present a quantitative analysis of the position-dependent contribution of all 20 amino acids to membrane insertion efficiency, as well as of the effects of transmembrane segment length and flanking amino acids. The emerging picture of translocon-mediated transmembrane helix assembly is simple, with the critical sequence characteristics mirroring the physical properties of the lipid bilayer.

Date: 2007
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DOI: 10.1038/nature06387

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