Cell-free translation of paramyxovirus messenger RNA.
Polypeptides corresponding in electrophoretic mobility to virion polypeptides 1, 3, and 5 were made in a reticulocyte cell-free system to which 18S RNA from Sendai virus-infected cells was added. Immune precipitation was used to select relevant polypeptides from endogenous products. The cell-free product corresponding to virion polypeptide 3 (the nucleocapsid structure unit) was the most abundant; its tryptic peptides comigrated electrophoretically with tryptic peptides of polypeptide 3 isolated from virions. Other sedimenting classes of RNA from infected cells were tested; only the 28S fraction showed slight activity. Virion 50S RNA was inactive. These findings support the hypothesis that complementary RNA transcripts of paramyxovirion RNA are the templates for viral proteins.
D000818:Animals; D002250:Carbon Radioisotopes; D002460:Cell Line; D002474:Cell-Free System; D002478:Cells, Cultured; D002642:Chick Embryo; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008168:Lung; D010222:Parainfluenza Virus 1, Human / Q000276:immunology / Q000378:metabolism*; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification; D011233:Precipitin Tests; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D011817:Rabbits / Q000276:immunology; D014357:Trypsin; D014764:Viral Proteins / Q000096:biosynthesis*
D002250:Carbon Radioisotopes; D010455:Peptides; D012333:RNA, Messenger; D012367:RNA, Viral; D014764:Viral Proteins; D014357:Trypsin