Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin.

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Abstract
Previous studies showed that the glycoportein (G) of vesicular stomatitis virus is synthesized in association with the endoplasmic reticulum (ER) membrane and that all G mRNA co-fractionates with ER membrane. Treatment of infected cells with puromycin results in dissociation of G mRNA and presumably the associated ribosomes from the ER membrane. Even if extracts from treated [Chinese hamster ovary CHO] cells are kept at low ionic strength (0.01 M KCl), over 80% of G mRNA is found unattached to membranes. There is no evidence for direct interaction of G mRNA with membranes; rather, the linkage apparently is mediated by the nascent G polypeptide.