A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.

The eukaryotic cytoskeleton is essential for structural support and intracellular transport, and is therefore a common target of animal pathogens. However, no phytopathogenic effector has yet been demonstrated to specifically target the plant cytoskeleton. Here we show that the Pseudomonas syringae...

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Main Authors: Amy Huei-Yi Lee, Brenden Hurley, Corinna Felsensteiner, Carmen Yea, Wenzislava Ckurshumova, Verena Bartetzko, Pauline W Wang, Van Quach, Jennifer D Lewis, Yulu C Liu, Frederik Börnke, Stephane Angers, Andrew Wilde, David S Guttman, Darrell Desveaux
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-02-01
Series:PLoS Pathogens
Online Access:http://europepmc.org/articles/PMC3271077?pdf=render
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spelling doaj-bcaba23c9a144a24ac9fa98d45b6f7b22020-11-24T21:26:04ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742012-02-0182e100252310.1371/journal.ppat.1002523A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.Amy Huei-Yi LeeBrenden HurleyCorinna FelsensteinerCarmen YeaWenzislava CkurshumovaVerena BartetzkoPauline W WangVan QuachJennifer D LewisYulu C LiuFrederik BörnkeStephane AngersAndrew WildeDavid S GuttmanDarrell DesveauxThe eukaryotic cytoskeleton is essential for structural support and intracellular transport, and is therefore a common target of animal pathogens. However, no phytopathogenic effector has yet been demonstrated to specifically target the plant cytoskeleton. Here we show that the Pseudomonas syringae type III secreted effector HopZ1a interacts with tubulin and polymerized microtubules. We demonstrate that HopZ1a is an acetyltransferase activated by the eukaryotic co-factor phytic acid. Activated HopZ1a acetylates itself and tubulin. The conserved autoacetylation site of the YopJ / HopZ superfamily, K289, plays a critical role in both the avirulence and virulence function of HopZ1a. Furthermore, HopZ1a requires its acetyltransferase activity to cause a dramatic decrease in Arabidopsis thaliana microtubule networks, disrupt the plant secretory pathway and suppress cell wall-mediated defense. Together, this study supports the hypothesis that HopZ1a promotes virulence through cytoskeletal and secretory disruption.http://europepmc.org/articles/PMC3271077?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Amy Huei-Yi Lee
Brenden Hurley
Corinna Felsensteiner
Carmen Yea
Wenzislava Ckurshumova
Verena Bartetzko
Pauline W Wang
Van Quach
Jennifer D Lewis
Yulu C Liu
Frederik Börnke
Stephane Angers
Andrew Wilde
David S Guttman
Darrell Desveaux
spellingShingle Amy Huei-Yi Lee
Brenden Hurley
Corinna Felsensteiner
Carmen Yea
Wenzislava Ckurshumova
Verena Bartetzko
Pauline W Wang
Van Quach
Jennifer D Lewis
Yulu C Liu
Frederik Börnke
Stephane Angers
Andrew Wilde
David S Guttman
Darrell Desveaux
A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
PLoS Pathogens
author_facet Amy Huei-Yi Lee
Brenden Hurley
Corinna Felsensteiner
Carmen Yea
Wenzislava Ckurshumova
Verena Bartetzko
Pauline W Wang
Van Quach
Jennifer D Lewis
Yulu C Liu
Frederik Börnke
Stephane Angers
Andrew Wilde
David S Guttman
Darrell Desveaux
author_sort Amy Huei-Yi Lee
title A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
title_short A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
title_full A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
title_fullStr A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
title_full_unstemmed A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
title_sort bacterial acetyltransferase destroys plant microtubule networks and blocks secretion.
publisher Public Library of Science (PLoS)
series PLoS Pathogens
issn 1553-7366
1553-7374
publishDate 2012-02-01
description The eukaryotic cytoskeleton is essential for structural support and intracellular transport, and is therefore a common target of animal pathogens. However, no phytopathogenic effector has yet been demonstrated to specifically target the plant cytoskeleton. Here we show that the Pseudomonas syringae type III secreted effector HopZ1a interacts with tubulin and polymerized microtubules. We demonstrate that HopZ1a is an acetyltransferase activated by the eukaryotic co-factor phytic acid. Activated HopZ1a acetylates itself and tubulin. The conserved autoacetylation site of the YopJ / HopZ superfamily, K289, plays a critical role in both the avirulence and virulence function of HopZ1a. Furthermore, HopZ1a requires its acetyltransferase activity to cause a dramatic decrease in Arabidopsis thaliana microtubule networks, disrupt the plant secretory pathway and suppress cell wall-mediated defense. Together, this study supports the hypothesis that HopZ1a promotes virulence through cytoskeletal and secretory disruption.
url http://europepmc.org/articles/PMC3271077?pdf=render
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