Location of sequences within rotavirus SA11 glycoprotein VP7 which direct it to the endoplasmic reticulum.
Open Access
- 1 July 1987
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 7 (7), 2491-2497
- https://doi.org/10.1128/mcb.7.7.2491
Abstract
The Simian 11 rotavirus glycoprotein VP7 is directed to the endoplasmic reticulum (ER) of the cell and retained as an integral membrane protein. The gene coding for VP7 predicts two potential initiation codons, each of which precedes a hydrophobic region of amino acids (H1 and H2) with the characteristics of a signal peptide. Using the techniques of gene mutagenesis and expression, we have determined that either hydrophobic domain alone can direct VP7 to the ER. A protein lacking both hydrophobic regions was not transported to the ER. Some polypeptides were directed across the ER membrane and then into the secretory pathway of the cell. For a variant retaining only the H1 domain, secretion was cleavage dependent, since an amino acid change which prevented cleavage also stopped secretion. However, secretion of two other deletion mutants lacking H1 and expressing truncated H2 domains was unaffected by this mutation, suggesting that these proteins were secreted without cleavage of their NH2-terminal hydrophobic regions or secreted after cleavage at a site(s) not predicted by current knowledge.This publication has 28 references indexed in Scilit:
- Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomesCell, 1986
- An internal signal sequence: The asialoglycoprotein receptor membrane anchorCell, 1986
- Deletions into an NH2-terminal hydrophobic domain result in secretion of rotavirus VP7, a resident endoplasmic reticulum membrane glycoprotein.The Journal of cell biology, 1985
- Multiple Mechanisms of Protein Insertion into and Across MembranesScience, 1985
- Signal sequencesJournal of Molecular Biology, 1985
- Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transportCell, 1985
- Patterns of Amino Acids near Signal‐Sequence Cleavage SitesEuropean Journal of Biochemistry, 1983
- Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNACell, 1983
- Mechanisms for the incorporation of proteins in membranes and organelles.The Journal of cell biology, 1982
- The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesisCell, 1981