Molecular code for transmembrane-helix recognition by the Sec61 translocon
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics2007 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 450, no 7172, 1026-1030 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2007. Vol. 450, no 7172, 1026-1030 p.
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:su:diva-25367DOI: 10.1038/nature06387ISI: 000251579900075OAI: oai:DiVA.org:su-25367DiVA: diva2:199609