Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 392, Issue 10

Issues

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

Kajohn Boonrod
  • RLP-AgroScience GmbH, AlPlanta-Institute for Plant Research, Breitenweg 71, D-67435 Neustadt, Germany
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marc W. Füllgrabe
  • RLP-AgroScience GmbH, AlPlanta-Institute for Plant Research, Breitenweg 71, D-67435 Neustadt, Germany
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Gabi Krczal
  • RLP-AgroScience GmbH, AlPlanta-Institute for Plant Research, Breitenweg 71, D-67435 Neustadt, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Michael Wassenegger
  • RLP-AgroScience GmbH, AlPlanta-Institute for Plant Research, Breitenweg 71, D-67435 Neustadt, Germany
  • Centre for Organismal Studies Heidelberg, University of Heidelberg, D-69120 Heidelberg, Germany
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2011-08-29 | DOI: https://doi.org/10.1515/BC.2011.097

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.

Keywords: autoproteolytic activity; helper component proteinase; site-directed mutagenesis

About the article

Corresponding author


Received: 2011-07-19

Accepted: 2011-07-20

Published Online: 2011-08-29

Published in Print: 2011-10-01


Citation Information: Biological Chemistry, Volume 392, Issue 10, Pages 937–945, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2011.097.

Export Citation

©2011 by Walter de Gruyter Berlin Boston.Get Permission

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Yayi Tu, Zhenqian Zhang, Daofeng Li, Heng Li, Jiangli Dong, Tao Wang, and Xiu-Qing Li
PLOS ONE, 2015, Volume 10, Number 8, Page e0136210
[2]
Yayi Tu, Yongsheng Jin, Dongyuan Ma, Heng Li, Zhenqian Zhang, Jiangli Dong, and Tao Wang
Scientific Reports, 2015, Volume 5, Page 15605

Comments (0)

Please log in or register to comment.
Log in