AGC kinase OsOxi1 positively regulates basal resistance through suppression of OsPti1a-mediated negative regulation

Hidenori Matsui, Muneo Yamazaki, Mitsuko Kishi-Kaboshi, Akira Takahashi, Hirohiko Hirochika

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

OsPti1a, a functional ortholog of tomato SlPti1, negatively regulates both basal resistance and R-gene-mediated resistance in rice. To investigate the molecular function of OsPti1a in defense responses, we searched for components interacting with OsPti1a using a yeast two-hybrid system. One of the interacting proteins is a Ser/Thr kinase that directly phosphorylates OsPti1a in vitro. This protein belongs to the AGC kinase family and is highly similar to AtOxi1, which is induced in response to a wide range of reactive oxygen species (ROS)-generating stimuli in Arabidopsis. Thus, it was designated OsOxi1. OsOxi1 was transiently phosphorylated in response to ROS and chitin elicitor. Both OsOxi1-overexpressing transgenic lines and the ospti1a mutant were highly sensitive to ROS treatment, indicating that OsOxi1 and OsPti1a are involved in ROS-mediated signaling in opposing ways. OsOxi1 is specifically expressed at infection sites where ROS are produced after inoculation with a blast fungus, Magnaporthe oryzae. Overexpression of OsOxi1 enhanced basal resistance to the blast fungus, indicating that OsOxi1 positively regulates disease resistance. OsOxi1 phosphorylates Thr-233 of OsPti1a and a point mutation of Thr-233 enhanced disease susceptibility to a bacterial pathogen Xanthomonas oryzae pv. oryzae (Xoo), suggesting that the phosphorylation of OsPti1a by OsOxi1 is essential for basal resistance to Xoo. Taken together, our data suggest that OsOxi1 positively regulates defense responses through the phosphorylation of OsPti1a, causing the release from an OsPti1a-dependent inhibition of the responses.

Original languageEnglish
Pages (from-to)1731-1744
Number of pages14
JournalPlant and Cell Physiology
Volume51
Issue number10
DOIs
Publication statusPublished - Oct 2010
Externally publishedYes

Keywords

  • AGC kinase
  • Basal resistance
  • Phosphorylation
  • Pto-interacting protein
  • ROS
  • Rice

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology

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