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Title: Analysis of the autoproteolytic activity of the recombinant helper component proteinase from zucchini yellow mosaic virus. Author: Boonrod K, Füllgrabe MW, Krczal G, Wassenegger M. Journal: Biol Chem; 2011 Oct; 392(10):937-45. PubMed ID: 21871010. 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.[Abstract] [Full Text] [Related] [New Search]