Cleavage of the cap binding protein complex polypeptide p220 is not effected by the second poliovirus protease 2A
作者： Richard E. Lloyd , Haruka Toyoda , Diane Etchison , Eckard Wimmer , Ellie Ehrenfeld
DOI: 10.1016/0042-6822(86)90291-6
关键词: Viral protein 、 Cleavage stimulation factor 、 Cleavage factor 、 Peptide sequence 、 Cleavage and polyadenylation specificity factor 、 Biochemistry 、 Cap-Binding Protein Complex 、 Protein biosynthesis 、 Biology 、 Cleavage (embryo) 、 Molecular biology 、 Virology
摘要: Abstract Poliovirus protein 2A contains a short amino acid sequence that also occurs in the putative active site of known viral proteinase, 3C, previously shown to be responsible for glutamine/glycine cleavages poliovirus polyprotein precursor. Experimental evidence indicates is second proteinase mediates cleavage two tyrosine/glycine generation virus-specific proteins. Since inhibition host cell synthesis correlates with specific 220,000-Da component cap binding complex, we have tested whether p220 activity. The results show (1) does not copurify activity, (2) partially purified fractions containing high activity contain no detectable sequences form either mature or precursor protein, and (3) anti-2A serum IgG inhibit vitro .
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