PKS5, a SNF1-related kinase, interacts with and phosphorylates NPR1, and modulates expression of WRKY38 and WRKY62

a.
College of Life Sciences, Peking University, Beijing 100871, China
b.
National Institute of Biological Sciences, Beijing 102206, China

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Corresponding author: E-mail address: xiechanggen@nibs.ac.cn (Changgen Xie)

摘要

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Abstract: NPR1 (Nonexpressor of Pathogenesis-Related gene 1) is a major co-activator of plant defense. Phosphorylations of NPR1 play important roles in fine-tuning its activity, however a kinase corresponding to such modification remains uncharacterized. Here, we report that NPR1 interacts with PKS5 (SOS2-like Protein Kinase 5). The AKR (AnKyrin Repeats) motif of NPR1 is required for this interaction. PKS5 phosphorylates NPR1 at the C-terminal region. Expression of PKS5 is induced quickly by Pseudomonas syringae pv. tomato DC3000. Expression level of two NPR1 target genes, WRKY38 and WRKY62, is reduced and/or delayed in pks5 mutants. Moreover, the expression of WRKY38 and WRKY62 displays a similar pattern in npr1-1pks5-1 double mutant comparing to that in npr1-1. Our results suggest that PKS5 functions at the upstream of NPR1 and might mediate expression of WRKY38 and WRKY62 possibly by interacting with and phosphorylating NPR1.
- phosphorylation /
- kianse /
- AKR /
- co-immunoprecipitation /
- NPR1

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