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A Bacterial Inhibitor of Host Programmed Cell Death Defenses Is an E3 Ubiquitin Ligase
Radmila Janjusevic,1*
Robert B. Abramovitch,2,3*
Gregory B. Martin,2,3
C. Erec Stebbins1
Abstract:
The Pseudomonas syringae protein AvrPtoB is translocated intoplant cells, where it inhibits immunity-associated programmedcell death (PCD). The structure of a C-terminal domain of AvrPtoBthat is essential for anti-PCD activity reveals an unexpectedhomology to the U-box and RING-finger components of eukaryoticE3 ubiquitin ligases, and we show that AvrPtoB has ubiquitinligase activity. Mutation of conserved residues involved inthe binding of E2 ubiquitinconjugating enzymes abolishesthis activity in vitro, as well as anti-PCD activity in tomatoleaves, which dramatically decreases virulence. These resultsshow that Pseudomonas syringae uses a mimic of host E3 ubiquitinligases to inactivate plant defenses.
1 Laboratory of Structural Microbiology, The Rockefeller University, New York, NY 10021, USA. 2 Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA. 3 Department of Plant Pathology, Cornell University, Ithaca, NY 14853, USA.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: stebbins{at}rockefeller.edu (C.E.S.); gbm7{at}cornell.edu (G.B.M.)
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