Abstract
Upon delivery to the plant cell during infection, the Pseudomonas syringae effector protein AvrRpt2 undergoes proteolytic processing, enhances pathogen virulence and causes the elimination of the Arabidopsis RIN4 protein. A structure-prediction method was employed in order to investigate possible biochemical functions of AvrRpt2. Results of a secondary structure prediction algorithm suggest that the functional C-terminal portion of AvrRpt2 is a cysteine protease. Mutation of predicted catalytic residues within this portion of AvrRpt2 abolished in planta processing, elimination of Arabidopsis RIN4, and the ability to trigger an RPS2-specific resistance response. These data indicate that AvrRpt2 is most likely a sequence divergent cysteine protease whose activity is required for elimination of RIN4 during infection.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Arabidopsis / immunology
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Arabidopsis / metabolism
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Arabidopsis / microbiology
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Arabidopsis Proteins / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism*
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Carrier Proteins / metabolism
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Catalytic Domain
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Cysteine Endopeptidases* / chemistry
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Cysteine Endopeptidases* / genetics
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Cysteine Endopeptidases* / metabolism
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DNA, Bacterial / genetics
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Electrophoresis, Polyacrylamide Gel
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Gene Expression
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Immunoblotting
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Intracellular Signaling Peptides and Proteins
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Protein Structure, Secondary
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Pseudomonas / enzymology*
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Pseudomonas / genetics*
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Pseudomonas / pathogenicity
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Structural Homology, Protein
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Transformation, Bacterial / genetics
Substances
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Arabidopsis Proteins
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Bacterial Proteins
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Carrier Proteins
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DNA, Bacterial
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Intracellular Signaling Peptides and Proteins
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RIN4 protein, Arabidopsis
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RPS2 protein, Arabidopsis
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avrRpt2 protein, Pseudomonas syringae
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Cysteine Endopeptidases