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_22
Snippet: Thus it appeared that with these deletions, the mutant VP7 proteins reached the Golgi apparatus. Mutant 51-61, whose deletion removed a region distal to the hydrophobic domains, exhibited a staining pattern identical to the wild-type, that of reticular staining and a perinuclear distribution distinct from that of the R-WGA staining pattern. It appears that the absence of the region coding for these amino acids was not sufficient to cause movement.....
Document: Thus it appeared that with these deletions, the mutant VP7 proteins reached the Golgi apparatus. Mutant 51-61, whose deletion removed a region distal to the hydrophobic domains, exhibited a staining pattern identical to the wild-type, that of reticular staining and a perinuclear distribution distinct from that of the R-WGA staining pattern. It appears that the absence of the region coding for these amino acids was not sufficient to cause movement of VP7 out of the ER to the Golgi apparatus.
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