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

  • Kajohn Boonrod , Marc W. Füllgrabe , Gabi Krczal and Michael Wassenegger EMAIL logo
Published/Copyright: August 29, 2011

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.


Corresponding author

Received: 2011-7-19
Accepted: 2011-7-20
Published Online: 2011-8-29
Published in Print: 2011-10-1

©2011 by Walter de Gruyter Berlin Boston

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