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

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...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1977
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110081/
https://www.ncbi.nlm.nih.gov/pubmed/195964
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collection PubMed
description 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.
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spelling pubmed-21100812008-05-01 Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin J Cell Biol Articles 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. The Rockefeller University Press 1977-08-01 /pmc/articles/PMC2110081/ /pubmed/195964 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin
title Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin
title_full Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin
title_fullStr Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin
title_full_unstemmed Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin
title_short Binding of viral glycoprotein mRNA to endoplasmic reticulum membranes is disrupted by puromycin
title_sort binding of viral glycoprotein mrna to endoplasmic reticulum membranes is disrupted by puromycin
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110081/
https://www.ncbi.nlm.nih.gov/pubmed/195964

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