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Science 24 November 2000:
Vol. 290. no. 5496, pp. 1594 - 1597
DOI: 10.1126/science.290.5496.1594

Reports

Disruption of Signaling by Yersinia Effector YopJ, a Ubiquitin-Like Protein Protease

Kim Orth,1 Zhaohui Xu,1 Mary Beth Mudgett,2 Zhao Qin Bao,1 Lance E. Palmer,3 James B. Bliska,3 Walter F. Mangel,4 Brian Staskawicz,2 Jack E. Dixon1*

Homologs of the Yersinia virulence effector YopJ are found in both plant and animal bacterial pathogens, as well as plant symbionts. These YopJ family members were shown to act as cysteine proteases. The catalytic triad of the protease was required for inhibition of the mitogen-activated protein kinase (MAPK) and nuclear factor kappa B (NF-kappa B) signaling in animal cells and for induction of localized cell death in plants. The substrates for YopJ were shown to be highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ family members exert their pathogenic effect on cells by disrupting this posttranslational modification.

1 Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA.
2 Department of Plant and Microbial Biology, University of California Berkeley, Berkeley, CA 94720-3102, USA.
3 Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, New York 11794-5222, USA.
4 Department of Biology, Brookhaven National Laboratory, Upton, NY 11973-5000, USA.
*   To whom correspondence should be addressed. E-mail: jedixon{at}umich.edu


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