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The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane

Eusebio, A. and Friedberg, T. and Spiess, M.. (1998) The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane. Experimental cell research, Vol. 241, H. 1. pp. 181-185.

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Official URL: http://edoc.unibas.ch/dok/A5258066

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Abstract

The orientation of signal sequences during insertion into the endoplasmic reticulum membrane is largely determined by the charged residues flanking the apolar domain. Using recombinant and mutant proteins, also length and hydrophobicity of the apolar segment were shown to affect the orientation: translocation of the N-terminus was found to be favored by long hydrophobic sequences, and translocation of the C-terminus, by short ones. Here, we tested the physiological significance of this phenomenon by mutagenesis of the hydrophobic portion of two natural signals with unusual flanking charges. Extending the hydrophobic domain of the short, cleaved Ncyt/Cexo signal of pre-provasopressin-neurophysin II and shortening that of the Nexo/Ccyt signal anchor of microsomal epoxide hydrolase resulted in a significant fraction of polypeptides inserting in the opposite orientation to that of the wild-type proteins. The topogenic contribution of the hydrophobic domain is thus important for the correct and uniform orientation of natural proteins and can explain the behavior of some of the signals with unusual flanking charges.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Spiess)
UniBasel Contributors:Spiess, Martin
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:0014-4827
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:19

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