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A Bacterial Acetyltransferase Destroys Plant Microtubule Networks and Blocks Secretion
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 B?rnke  Stephane Angers  Andrew Wilde  David S Guttman  Darrell Desveaux
Abstract: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.
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