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The AvrPphB effector of Pseudomonas syringae is a papain-like protease that is injected into the host plant cell and cleaves specific kinases to disrupt immune signaling. Here, we used the unique substrate specificity of AvrPphB to generate a specific activity-based probe. This probe displays various AvrPphB isoforms in bacterial extracts, upon secretion and inside the host plant. We show that AvrPphB is secreted as a proprotease and that secretion requires the prodomain, but probably does not involve a pH-dependent unfolding mechanism. The prodomain removal is required for the ability of AvrPphB to trigger a hypersensitive cell death in resistant host plants, presumably since processing exposes a hidden acylation site required for subcellular targeting in the host cell. We detected two active isoforms of AvrPphB in planta, of which the major one localizes exclusively to membranes.

Original publication

DOI

10.1016/j.chembiol.2012.11.007

Type

Journal article

Journal

Chem Biol

Publication Date

21/02/2013

Volume

20

Pages

168 - 176

Keywords

Amino Acid Sequence, Arabidopsis, Bacterial Proteins, Hydrogen-Ion Concentration, Molecular Probes, Molecular Sequence Data, Protein Isoforms, Protein Structure, Tertiary, Pseudomonas syringae, Recombinant Proteins, Substrate Specificity