Skip to main page content
U.S. flag

An official website of the United States government

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2007 Dec 13;450(7172):1026-30.
doi: 10.1038/nature06387.

Molecular code for transmembrane-helix recognition by the Sec61 translocon

Tara Hessa  1 , Nadja M Meindl-Beinker, Andreas Bernsel, Hyun Kim, Yoko Sato, Mirjam Lerch-Bader, IngMarie Nilsson, Stephen H White, Gunnar von Heijne
Affiliations

Molecular code for transmembrane-helix recognition by the Sec61 translocon

Tara Hessa et al. Nature. .

Abstract

Transmembrane alpha-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.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types