๐ Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus
In the eukaryotic cell, both secreted and plasma membrane proteins are synthesized at the endoplasmic reticulum, then transported, via the Golgi complex, to the cell surface1-4. Each of the compartments of this transport pathway carries out particular metabolic functions5-8, and therefore presumably contains a distinct complement of membrane proteins. Thus, mechanisms must exist for localizing such proteins to their respective destinations. However, a major obstacle to the study of such mechanisms is that the isolation and detailed analysis of such internal membrane proteins pose formidable technical problems. We have therefore used the E1 glycoprotein from coronavirus MHV-A59 as a viral model for this class of protein. Here we present the primary structure of the protein, determined by analysis of cDNA clones prepared from viral mRNA. In combination with a previous study of its assembly into the endoplasmic reticulum membrane9, the sequence reveals several unusual features of the protein which may be related to its intracellular localization. ยฉ 1984 Nature Publishing Group.
author
๐ค Armstrong, John
๐ค Niemann, Heiner
๐ค Smeekens, Sjef
๐ค Rottier, Peter
๐ค Warren, Graham
year
โฐ 1984
journal
๐ Nature
issn
๐ 00280836
volume
308
number
5961
page
751-752
citedbycount
81
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