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Title: A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion

item LEE, AHY - University Of Toronto
item HURLEY, B - University Of Toronto
item FELSENSTEINER, C - University Of Toronto
item YEA, C - University Of Toronto
item CKURSHUMOVA, W - University Of Toronto
item BARTETZKO, V - Friedrich-Alexander University
item WANG, P - University Of Toronto
item QUACH, V - University Of Toronto
item Lewis, Jennifer
item LIU, Y - University Of Toronto
item BORNKE, F - Friedrich-Alexander University
item ANGERS, S - University Of Toronto
item WILDE, A - University Of Toronto
item GUTTMAN, D - University Of Toronto
item DESVEAUX, D - University Of Toronto

Submitted to: PLoS Pathogens
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/20/2011
Publication Date: 2/2/2012
Citation: Lee, A., Hurley, B., Felsensteiner, C., Yea, C., Ckurshumova, W., Bartetzko, V., Wang, P.W., Quach, V., Lewis, J.D., Liu, Y.C., Bornke, F., Angers, S., Wilde, A., Guttman, D.S., Desveaux, D. 2012. A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion. PLoS Pathogens. 8(2): e1002523.

Interpretive Summary: Many bacterial pathogens disrupt key components of host physiology by injecting virulence proteins (or “effectors”) via a needle-like structure, called the type III secretion system, directly into eukaryotic cells. The YopJ / HopZ superfamily of type III secreted effector proteins is found in pathogens of both animals and plants providing an excellent opportunity to address how a family of type III secreted effectors can promote pathogenesis in hosts from two kingdoms. YopJ from the animal pathogen Yersinia pestis is an acetyltransferase that targets signaling components of innate immunity and prevents their activation. Here we show that HopZ1a, from the phytopathogen Pseudomonas syringae is an acetyltransferase that binds plant tubulin. Like YopJ, the eukaryotic cofactor phytic acid activates the acetyltransferase activity of HopZ1a. In addition, we demonstrate that activated HopZ1a can acetylate tubulin, a major constituent of the eukaryotic cytoskeleton. In plants, activated HopZ1a causes a dramatic destruction of microtubule networks, inhibits protein secretion, and ultimately suppresses cell wall-mediated defense. Our study emphasizes the functional diversification of this important type III effector family in plant and animal hosts using a conserved acetyltransferase activity.

Technical 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.