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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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
29. August 2011
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| In: |
Biological chemistry
Year: 2011, Volume: 392, Issue: 10, Pages: 937-945 |
| ISSN: | 1437-4315 |
| DOI: | 10.1515/BC.2011.097 |
| Online Access: | 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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| Author Notes: | Kajohn Boonrod, Marc W. Füllgrabe, Gabi Krczal and Michael Wassenegger |
| Summary: | 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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| Item Description: | Gesehen am 02.06.2022 |
| Physical Description: | Online Resource |
| ISSN: | 1437-4315 |
| DOI: | 10.1515/BC.2011.097 |