作者: P L Whitfeld , C Tyndall , S C Stirzaker , A R Bellamy , G W Both
DOI: 10.1128/MCB.7.7.2491
关键词: Biology 、 Endoplasmic reticulum 、 Signal peptide 、 Peptide sequence 、 Secretion 、 Integral membrane protein 、 Glycoprotein 、 Secretory pathway 、 Membrane protein 、 Molecular biology
摘要: The Simian 11 rotavirus glycoprotein VP7 is directed to the endoplasmic reticulum (ER) of cell and retained as an integral membrane protein. gene coding for predicts two potential initiation codons, each which precedes a hydrophobic region amino acids (H1 H2) with characteristics signal peptide. Using techniques mutagenesis expression, we have determined that either domain alone can direct ER. A protein lacking both regions was not transported Some polypeptides were across ER then into secretory pathway cell. For variant retaining only H1 domain, secretion cleavage dependent, since acid change prevented also stopped secretion. However, other deletion mutants expressing truncated H2 domains unaffected by this mutation, suggesting these proteins secreted without their NH2-terminal or after at site(s) predicted current knowledge.