Poliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro
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Summary
It is concluded that 3C is merely the core of the Gln-Gly-cleaving activity which processes P1 in vivo and that there is probably a hydrophobic contact between a larger 3C precursor and its P1 substrate which allows the second processing reaction: 1ABC, 1D----1AB, 1C,1D.
- Type
- article
- Published
- 1988-12-01
- Cited by
- 90
- References
- 33
- Access
- Open access
- OpenAlex
- https://openalex.org/W1918993077
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19757635
Keywords
Capsid, Biology, Cleavage (geology), Recombinant DNA, In vitro
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- In vitro molecular genetics as a tool for determining the differential cleavage specificities of the poliovirus 3C proteinase.
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- Implications of the picornavirus capsid structure for polyprotein processing.
- A detailed kinetic analysis of the in vitro synthesis and processing of encephalomyocarditis virus products.
- Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme.
- Myristylation of picornavirus capsid protein VP4 and its structural significance
- A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein.
- Primary structure, gene organization and polypeptide expression of poliovirus RNA
Cited by
- Mutational analysis of the proposed FG loop of poliovirus proteinase 3C identifies amino acids that are necessary for 3CD cleavage and might be determinants of a function distinct from proteolytic activity
- Specificity of the polioviral proteinase 3C towards genetically engineered cleavage sites in the viral capsid.
- Mengo virus 3C proteinase: Recombinant expression, intergenus substrate cleavage and localizationin vivo
- Picornavirus protein processing--enzymes, substrates, and genetic regulation.
- Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase
- Identification of the cleavage site and determinants required for poliovirus 3CPro-catalyzed cleavage of human TATA-binding transcription factor TBP
- Inhibition of basal transcription by poliovirus: a virus- encoded protease (3Cpro) inhibits formation of TBP-TATA box complex in vitro
- Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli
- Expression of poliovirus nonstructural proteins in Escherichia coli cells. Modification of membrane permeability induced by 2B and 3A.
- Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity
- Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificity
- Regulation of Gene Expression in Animal Viruses
- Infection of HeLa cells with poliovirus results in modification of a complex that binds to the rRNA promoter
- Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase
- Picornains 2A and 3C.
- Effects of mutations in poliovirus 3Dpol on RNA polymerase activity and on polyprotein cleavage
- trans rescue of a mutant poliovirus RNA polymerase function
- Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro
- Poliovirus assembly and encapsidation of genomic RNA.
- Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
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