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

• Verfasst von: Kajohn Boonrod [VerfasserIn]
• Verfasst von: Füllgrabe, Marc W. [VerfasserIn]
• Verfasst von: Krczal, Gabi [VerfasserIn]
• Verfasst von: Wassenegger, Michael [VerfasserIn]
• Titel: Analysis of the autoproteolytic activity of the recombinant helper component proteinase from zucchini yellow mosaic virus
• Verf.angabe: Kajohn Boonrod, Marc W. Füllgrabe, Gabi Krczal and Michael Wassenegger
• E-Jahr: 2011
• Jahr: 29. August 2011
• Umfang: 9 S.
• Fussnoten: Gesehen am 02.06.2022
• Titel Quelle: Enthalten in: Biological chemistry
• Ort Quelle: Berlin [u.a.] : de Gruyter, 1996
• Jahr Quelle: 2011
• Band/Heft Quelle: 392(2011), 10, Seite 937-945
• ISSN Quelle: 1437-4315
• DOI: doi:10.1515/BC.2011.097
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: autoproteolytic activity
• Sach-SW: helper component proteinase
• Sach-SW: site-directed mutagenesis
• K10plus-PPN: 1805739166

Abstract

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.