Identification of the cleavage site and determinants required for poliovirus 3CPro-catalyzed cleavage of human TATA-binding transcription factor TBP.

摘要: Abstract Host cell RNA polymerase II-mediated transcription is inhibited by poliovirus infection. We have shown previously that the human TATA-binding protein (TBP), a general factor required for of all II genes, directly cleaved both in vitro and vivo virus-coded protease 3CPro. 3CPro specifically cleaves glutamine-glycine bonds viral polyprotein. Cellular TBP contains three sites, at amino acids 12, 18, 108. By using site-directed mutagenesis, we determined bond acid but not 12 or 108, protease. Both glutamine glycine appear to be important cleavage. Further mutations around site position 18 suggest determinants other than are also 3CPro-induced An alanine P4 proline P2, proximal scissile pair, 3CPro-mediated cleavage TBP. Our results specificity cellular very similar its mode polyproteins.