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.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Boonrod K,Füllgrabe MW,Krczal G,Wassenegger Mdoi
10.1515/BC.2011.097subject
Has Abstractpub_date
2011-10-01 00:00:00pages
937-45issue
10eissn
1431-6730issn
1437-4315journal_volume
392pub_type
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