Proceedings of the National Academy of Sciences · 1981 · 90 citations · 28 references
Life SciencesBiologyMolecular BiologyMolecular VirologyProtein BiochemistryVirologyProteolytic EnzymesProteolytic ProcessingViral Protein ProcessingViral ReplicationViral Rna BiologyVirus Genome OrganizationProtease Cleavage Site PredictionProtease Cleavage SitesProteolytic Cleavage Of Viral PolyproteinsProteolytic Processing AnalysisProteolytic Processing Of Viral Structural ProteinsViral Polyprotein ProcessingViral ProteasesViral Replication Protein Processing
A partial amino-terminal amino acid sequence of each of the major proteins encoded by the replicase region (P3) of the poliovirus genome has been determined. A comparison of this sequence information with the amino acid sequence predicted from the RNA sequence that has been determined for the 3' region of the poliovirus genome has allowed us to locate precisely the proteolytic cleavage sites at which the initial polyprotein is processed to create the poliovirus products P3-1b (NCVP1b), P3-2 (NCVP2), P3-4b (NCVP4b), and P3-7c (NCVP7c). For each of these products, as well as for the small genome-linked protein VPg, proteolytic cleavage occurs between a glutamine and a glycine residue to create the amino terminus of each protein. This result suggests that a single proteinase may be responsible for all of these cleavages. The sequence data also allow the precise positioning of the genome-linked protein VPg within the precursor P3-1b just proximal to the amino terminus of polypeptide P3-2.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Proteases and biological control
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