title: Translation of individual species of vesicular stomatitis viral mRNA.
abstract: Vesicular stomatitis virus mRNAs from three of the four bands fractionated by polyacrylamide gel electrophoresis in 99% formamide have been eluted from gels and translated in the Krebs II ascites cell-free system. Band 2 mRNA (0.7 times 10-6 daltons) directed the synthesis of the protein moiety of the glycoprotein (G), and band 3 (0.55 times 10-6 daltons) coded for the nucleocapsid (N) protein. Band 4 mRNA (o.28 times 10-6 daltons) directed the synthesis of the NS and matrix (M) proteins. The authenticity of viral proteins synthesized in vitro was shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by analysis of (35-S)metionine-labeled tryptic peptides. These results are consistent with the complexity analysis and coding capacities for the vesicular stomatitis virus mRNA species presented in the accompanying paper.
mesh_terms: D000818:Animals; D001345:Autoradiography; D002287:Carcinoma, Krebs 2; D002474:Cell-Free System; D004591:Electrophoresis, Polyacrylamide Gel; D008715:Methionine; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000032:analysis*; D012367:RNA, Viral / Q000032:analysis*; D013462:Sulfur Radioisotopes; D014357:Trypsin; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis
chemical_list: D010455:Peptides; D012333:RNA, Messenger; D012367:RNA, Viral; D013462:Sulfur Radioisotopes; D014764:Viral Proteins; D008715:Methionine; D014357:Trypsin