Jan 14, 2014

Identification of a plant kinase that phosphorylates the bacterial effector AvrPtoB

BioRxiv : the Preprint Server for Biology
Katie LeachNeil Reid

Abstract

A critical component controlling bacterial virulence is the delivery of pathogen effectors into plant cells during infection. Effectors alter host metabolism and immunity for pathogen benefit. Multiple effectors are phosphorylated by host kinases, and this posttranslational modification is important for their activity. We sought to identify host kinases involved in effector phosphorylation. Multiple effector phosphorylated residues matched the proposed consensus phosphorylation motif of the plant calcium-dependent protein kinase (CDPK) and Snf1-related kinase (SnRK) superfamily. The conserved Pseudomonas effector AvrPtoB acts as an E3 ubiquitin ligase and promotes bacterial virulence. We identified a member of the Arabidopsis SnRK family, SnRK2.8, that associated with AvrPtoB in yeast and in planta. SnRK2.8 was required for AvrPtoB virulence functions, including facilitating bacterial colonization, suppression of callose deposition, and targeting the plant defense regulator NPR1 and flagellin receptor FLS2. Mass spectrometry revealed AvrPtoB was phosphorylated at multiple serine residues in planta, with S258 phosphorylation reduced in the snrk2.8 knockout. AvrPtoB phospho-null mutants exhibited compromised virulence functions a...Continue Reading

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Mentioned in this Paper

Impacted Tooth
Contraction (Finding)
Phylogenetic Analysis
Subgenus Pika
Evaluation
Objective (Goal)
Lagomorpha
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Species
Disease Regression

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