Analysis of the autoproteolytic activity of the recombinant helper component proteinase from zucchini yellow mosaic virus

The multifunctional helper component proteinase (HC-Pro) of potyviruses contains an autoproteolytic function that, together with the protein 1 (P1) and NIa proteinase, processes the polyprotein into mature proteins. In this study, we analysed the autoproteolytic active domain of zucchini yellow mosa...

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Hauptverfasser: Kajohn Boonrod (VerfasserIn) , Füllgrabe, Marc W. (VerfasserIn) , Krczal, Gabi (VerfasserIn) , Wassenegger, Michael (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 29. August 2011
In: Biological chemistry
Year: 2011, Jahrgang: 392, Heft: 10, Pages: 937-945
ISSN:1437-4315
DOI:10.1515/BC.2011.097
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1515/BC.2011.097
Verlag, lizenzpflichtig, Volltext: https://www.degruyterbrill.com/document/doi/10.1515/BC.2011.097/html
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Verfasserangaben:Kajohn Boonrod, Marc W. Füllgrabe, Gabi Krczal and Michael Wassenegger

MARC

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520 |a The multifunctional helper component proteinase (HC-Pro) of potyviruses contains an autoproteolytic function that, together with the protein 1 (P1) and NIa proteinase, processes the polyprotein into mature proteins. In this study, we analysed the autoproteolytic active domain of zucchini yellow mosaic virus (ZYMV) HC-Pro. Several Escherichia coli -expressed MBP:HC-Pro:GFP mutants containing deletions or point mutations at either the N- or C-terminus of the HC-Pro protein were examined. Our results showed that amino acids essential for the proteolytic activity of ZYMV HC-Pro are distinct from those of the tobacco etch virus HC-Pro, although the amino acid sequences in the proteolytic active domain are conserved among potyviruses. 
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