Frog oocytes synthesize and completely process the precursor polypeptide to virion structural proteins after microinjection of avian myeloblastosis virus RNA.
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.
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
D012367:RNA, Viral; D014764:Viral Proteins