Relationship between synthesis and cleavage of poliovirus-specific proteins.
Poliovirus proteinase was studied in vitro in lysates from poliovirus-infected HeLa cells. Preincubation of these lysates caused (i) a reduction in poliovirus proteinase activity and (ii) a partial dependence on exogenous mRNA for optimal translation. Proteins translated from endogenous poliovirus RNA in preincubated extracts from virus-infected HeLa cells are poorly cleaved. This cleavage deficiency is alleviated by adding fresh poliovirus RNA to the translation system, thus, allowing re-initiation to occur. This suggests that the poliovirus proteinase is highly unstable.
D010450:Endopeptidases / Q000378:metabolism*; D006367:HeLa Cells; D010442:Peptide Chain Initiation, Translational; D017955:Poliovirus / Q000378:metabolism*; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000378:metabolism; D012367:RNA, Viral / Q000235:genetics; D014764:Viral Proteins / Q000096:biosynthesis / Q000378:metabolism*
D011498:Protein Precursors; D012367:RNA, Viral; D014764:Viral Proteins; D010450:Endopeptidases