Abstract
The RNA genome of tobacco etch virus (TEV) encodes a large polyprotein precursor that is processed to mature proteins by virus-specific proteinases. Cleavage sites located within the carboxyl-terminal two-thirds of the polyprotein are processed by a TEV-encoded 49 kd proteinase, while the enzyme(s) responsible for cleaving the remaining sites has not been found. In this study, a second TEV-encoded proteinase has been identified based on cell-free expression of defined RNA transcripts. The boundaries of this proteinase have been delineated by deletion analysis and site-directed mutagenesis. The proteolytically active domain has been localized to the carboxyl-terminal half of the 56 kd aphid-transmission helper component. A cleavage site that is recognized by this proteinase has been identified in the polyprotein adjacent to the carboxyl-terminus of the enzyme, and the proteinase appears to cleave by an autocatalytic mechanism. Proteolysis in vitro occurs between a Gly-Gly dipeptide as determined by radiochemical sequencing at the amino-terminus of the proteolytic product.
MeSH Terms
Amino Acid Sequence
Binding Sites
Endopeptidases/genetics,metabolism
Genes, Viral
Molecular Sequence Data
Mutation
Plant Viruses/genetics,metabolism
Protein Precursors/metabolism
Protein Processing, Post-Translational
Chemicals
Protein Precursors
Endopeptidases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Carrington J C
Department of Biology, Texas A&M University, College Station 77843.
Cary S M
Parks T D
Dougherty W G
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