A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase

Science

Volumn 311, Issue 5758, 2006, Pages 222-226

  Janjusevic, Radmila ^a   Abramovitch, Robert B ^b,c   Martin, Gregory B ^b,c   Stebbins, C Erec ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b United States Department of Agriculture Agricultural Research Service and Boyce Thompson Institute for Plant Research   (United States)

^c Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELLS; ENZYME KINETICS; MUTAGENESIS; PLANTS (BOTANY);

BACTERIAL INHIBITORS; E3 UBIQUITIN LIGASE; HOMOLOGY; PROGRAMMED CELL DEATH (PCD);

ENZYME INHIBITION;

PROTEIN AVRPTOB; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

PROTEIN;

APOPTOSIS; ARTICLE; BACTERIAL VIRULENCE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME BINDING; HOST PATHOGEN INTERACTION; NONHUMAN; PLANT CELL; PLANT DEFENSE; PLANT LEAF; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TRANSPORT; PSEUDOMONAS SYRINGAE; SEQUENCE HOMOLOGY; TOMATO;

APOPTOSIS; BACTERIAL PROTEINS; HUMANS; LYCOPERSICON ESCULENTUM; MOLECULAR MIMICRY; MUTAGENESIS; PLANT DISEASES; PLANT LEAVES; PLANT PROTEINS; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; PSEUDOMONAS SYRINGAE; RECOMBINANT FUSION PROTEINS; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITIN-PROTEIN LIGASES;

BACTERIA (MICROORGANISMS); EUKARYOTA; LYCOPERSICON ESCULENTUM; PSEUDOMONAS SYRINGAE;

EID: 30844458212     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1120131     Document Type: Article

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34. We thank H. Mueller at Rockefeller University and T. Radhakannan, R. Ramagopal, and W. Shi of Brookhaven beamline X9A for access to and assistance with crystallographic equipment and R. Bennett, C. Pepper, A. Gazes, and G. Latter of Rockefeller University for computational facilities support. Protein N-terminal sequencing and mass-spectroscopic analysis were performed at the Rockefeller University under the direction of H. Deng. We thank D. Schneider for bioinformatics support and S. Manon of the Rockefeller Chemical Biology Spectroscopy Resource Center for access to circular dichroism equipment. We thank the Arabidopsis Biological Resource Center and donors of stock U09652: J. Ecker, A. Theologis, and R. Davis [SSP Consortium: Salk, Stanford, PGEC (Plant Gene Expression Center)]. This work was supported in part by a Burroughs-Welcome Investigators in Pathogenesis of Infectious Disease award and funds from the Rockefeller University to C.E.S., a fellowship from the Natural Sciences and Engineering Research Council of Canada to R.B.A., and funds from the Triad Foundation and the U.S. Department of Agriculture National Research Initiative to G.B.M. Coordinates have been deposited in the Protein Data Bank under PDB ID 2FD4.