Site of synthesis of membrane and nonmembrane proteins of vesicular stomatitis virus

• Published in: The Journal of biological chemistry Vol. 250; no. 17; pp. 6955 - 6962
• Main Author: Morrison, T G
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 10.09.1975
• Subjects: Amino Acids - analysis; Cell Line; Glycoproteins - biosynthesis; Membranes - metabolism; Methionine - metabolism; Peptide Fragments - analysis; Polyribosomes - metabolism; Polyribosomes - ultrastructure; Protein Biosynthesis; Vesicular stomatitis Indiana virus - metabolism; Viral Proteins - biosynthesis
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)41025-9

Upon infection of Chinese hamster ovary cells (CHO), vesicular stomatitis (VSV) virus synthesizes two membrane proteins (the VSV glycoprotein and the VSV matrix or membrane (M) protein) and three nonmembrane proteins (the VSV nucleocapsid, the viral transcriptase, and an NS protein). We have used the VSV-infected cell as a model system for the study of the site of synthesis of these membrane and nonmembrane proteins. We have isolated VSV mRNA from free polyribosomes, membrane-bound polyribosomes, and the postribosomal supernatant, and identified the individual species of VSV mRNA present in each fraction. The mRNA which encodes the VSV glycoprotein is found exclusively on membrane-bound polyribosomes, while the mRNAs which encode the VSV, M, N, and NS proteins are found in free polyribosomes, in the membrane fraction of the cell, and in the postribosomal supernatant. Our results suggest that the VSV glycoprotein is synthesized exclusively on membrane polyribosomes, while at least some of the M, N, and NS proteins are made on free polyribosomes.