Evidence of ambiguous processing and selective degradation in the noncapsid proteins of rhinovirus 1A.

摘要: Pulse-chase kinetics and extensive pactamycin mapping studies show that the translation of rhinovirus 1A proceeds in order: initiate-P1-S-P2-terminate, where P1 is precursor to capsid proteins, S a stable primary gene product, P2 family noncapsid products. Initial examination molar stoichiometry families rhinoviral proteins infected cells suggested both regions were translated more frequently than region. However, we this apparent asymmetry an artifact arising from two phenomena: (i) ambiguous cleavage sites which result alternative products region, having molecular weights 47,000 38,000, (ii) several fates for precursors, including degradation 35 45% small unidentifiable Another artifact, time-dependent shift position polypeptide r-39, was traced selective inhibition rate its (peak 76). The processing 92) not retarded by pactamycin.