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Multiple determinants direct the orientation of signal-anchor proteins : the topogenic role of the hydrophobic signal domain
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 153672
Author(s) Wahlberg, J M; Spiess, M
Author(s) at UniBasel Spiess, Martin
Year 1997
Title Multiple determinants direct the orientation of signal-anchor proteins : the topogenic role of the hydrophobic signal domain
Journal The Journal of cell biology
Volume 137
Number 3
Pages / Article-Number 555-62
Keywords Amino Acid Sequence; Animals; Asialoglycoprotein Receptor; Biological Transport; COS Cells; Cell Membrane/metabolism; Cercopithecus aethiops; Hexosaminidases/pharmacology; Leucine/chemistry; Membrane Glycoproteins/*metabolism; Molecular Sequence Data; Molecular Weight; Protein Sorting Signals/*chemistry; Receptors; Cell Surface/*metabolism; Solubility; Structure-Activity Relationship; Trypsin
Abstract The orientation of signal-anchor proteins in the endoplasmic reticulum membrane is largely determined by the charged residues flanking the apolar, membrane-spanning domain and is influenced by the folding properties of the NH2-terminal sequence. However, these features are not generally sufficient to ensure a unique topology. The topogenic role of the hydrophobic signal domain was studied in vivo by expressing mutants of the asialoglycoprotein receptor subunit H1 in COS-7 cells. By replacing the 19-residue transmembrane segment of wild-type and mutant H1 by stretches of 7-25 leucine residues, we found that the length and hydrophobicity of the apolar sequence significantly affected protein orientation. Translocation of the NH2 terminus was favored by long, hydrophobic sequences and translocation of the COOH terminus by short ones. The topogenic contributions of the transmembrane domain, the flanking charges, and a hydrophilic NH2-terminal portion were additive. In combination these determinants were sufficient to achieve unique membrane insertion in either orientation.
Publisher Rockefeller University Press
ISSN/ISBN 0021-9525
edoc-URL http://edoc.unibas.ch/dok/A5258067
Full Text on edoc Available
Digital Object Identifier DOI 10.1083/jcb.137.3.555
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/9151664
ISI-Number WOS:A1997WY01900003
Document type (ISI) Journal Article
 
   

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