Title: Deletions into an NH2-terminal hydrophobic domain result in secretion of rotavirus VP7, a resident endoplasmic reticulum membrane glycoprotein Document date: 1985_12_1
ID: zrv9fjgn_28
Snippet: Analysis of the amino acid sequence of VP7 has shown the existence of two tandem NH2-terminal hydrophobic domains, within the first 50 amino acids. Each is preceded by an inframe ATG codon. Since the first ATG is "weak" and the second one has the preferred consensus sequence for initiation (24) , we cannot be sure which one is used for VP7 synthesis, and are unable to say where the reported signal peptide cleavage occurs (13) . Since mutant 1-14,.....
Document: Analysis of the amino acid sequence of VP7 has shown the existence of two tandem NH2-terminal hydrophobic domains, within the first 50 amino acids. Each is preceded by an inframe ATG codon. Since the first ATG is "weak" and the second one has the preferred consensus sequence for initiation (24) , we cannot be sure which one is used for VP7 synthesis, and are unable to say where the reported signal peptide cleavage occurs (13) . Since mutant 1-14, which deletes the first ATG codon, still produces a glycoprotein located in the ER, the second hydrophobic domain can provide signal pep-PORUCHYNSKY lET AL.
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