Autocatalytic Processing of the Potyvirus Helper Component Proteinase in Escherichia coli and In Vitro Public Deposited

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  • The virus-encoded proteins of tobacco etch virus (TEV), a plant potyvirus, arise by proteolytic processing of a large polyprotein precursor. The TEV genome codes for two proteinases, a 49-kilodalton proteinase and helper component proteinase (HC-Pro), which cleave the polyprotein at specific sites. The only known cleavage event catalyzed by HC-Pro occurs at the HC-Pro carboxyl terminus. The proteolytic activity of HC-Pro was analyzed by expression of the enzyme in bacterial and cell-free systems. The carboxyl-terminal domain of HC-Pro exhibited proteolytic activity in Escherichia coli with a processing half-time of approximately 100 s. The processing kinetics of HC-Pro expressed in vitro by cell-free transcription and translation was variable, depending on the presence or absence of TEV polypeptide sequences at the amino terminus of the proteolytic domain. Cleavage of the HC-Pro carboxyl terminus appeared to proceed exclusively by an autocatalytic mechanism; the proteinase synthesized in vitro exhibited little or no proteolytic activity when reacted with the HC-Pro cleavage site in trans or bimolecular reactions.
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  • Carrington, J. C., Freed, D. D., & Sanders, T. C. (1989, October). Autocatalytic Processing of the Potyvirus Helper Component Proteinase in Escherichia coli and In Vitro. Journal of Virology, 63(10), 4459-4463
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  • description.provenance : Approved for entry into archive by Sue Kunda(sue.kunda@oregonstate.edu) on 2011-05-26T00:42:54Z (GMT) No. of bitstreams: 1 CarringtonJamesC.BotanyPlantPathology.AutocatalyticProcessingPotyvirus.pdf: 1727539 bytes, checksum: 5079c374160962f7ae7a32ff5b564829 (MD5)
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