title: Frog oocytes synthesize and completely process the precursor polypeptide to virion structural proteins after microinjection of avian myeloblastosis virus RNA.
abstract: After microinjection of Xenopus laevis oocytes with RNA from avian myeloblastosis virus, viral structural proteins p27, p19, p15, and p12 are formed by a sequence of posttranslational cleavages of a high-molecular-weight precursor polypeptide. The 60-70S RNA aggregate or its 30-40S RNA subunits obtained by heat or formamide treatment possess the same ability to serve as template in X. laevis oocytes. The processing pattern of virus-specific precursor polypeptides is the same in X. laevis oocytes as in chick embryo fibroblasts infected with avian myeloblastosis virus, but the processing takes place at a much slower rate.
mesh_terms: D000818:Animals; D001354:Avian Leukosis Virus / Q000378:metabolism*; D009189:Avian Myeloblastosis Virus / Q000378:metabolism*; D002642:Chick Embryo; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D008845:Microinjections; D008970:Molecular Weight; D009865:Oocytes / Q000378:metabolism*; D010063:Ovum / Q000378:metabolism*; D010452:Peptide Biosynthesis; D011233:Precipitin Tests; D014176:Protein Biosynthesis; D012367:RNA, Viral / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis*; D014981:Xenopus
chemical_list: D012367:RNA, Viral; D014764:Viral Proteins