title: Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin.
abstract: Previous studies showed that the glycoprotein (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. Here, we show that treatment of infected cells with puromycin results in dissociation of G mRNA, and presumably the associated ribosomes, from the ER membrane. Even it extracts from treated 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 GmRNA with membranes; rather, the linkage apparently is mediated by the nascent G polypeptide.
mesh_terms: D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D009994:Osmolar Concentration; D011691:Puromycin / Q000494:pharmacology*; D012333:RNA, Messenger / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis*
chemical_list: D012333:RNA, Messenger; D012367:RNA, Viral; D014764:Viral Proteins; D011691:Puromycin