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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2012-02-01
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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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