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Originally published in Science Express on 22 December 2005
Science 13 January 2006:
Vol. 311. no. 5758, pp. 222 - 226
DOI: 10.1126/science.1120131
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Reports

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{dagger} C. Erec Stebbins1{dagger}

The Pseudomonas syringae protein AvrPtoB is translocated into plant cells, where it inhibits immunity-associated programmed cell death (PCD). The structure of a C-terminal domain of AvrPtoB that is essential for anti-PCD activity reveals an unexpected homology to the U-box and RING-finger components of eukaryotic E3 ubiquitin ligases, and we show that AvrPtoB has ubiquitin ligase activity. Mutation of conserved residues involved in the binding of E2 ubiquitin–conjugating enzymes abolishes this activity in vitro, as well as anti-PCD activity in tomato leaves, which dramatically decreases virulence. These results show that Pseudomonas syringae uses a mimic of host E3 ubiquitin ligases 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.

{dagger} 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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