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Regulation of the Rice NADPH Oxidase by Binding of Small GTPase Rac and Ca2+ to Its N-terminal Extension

  • Hann Ling Wong
  • Reinhard Pinontoan
  • Kana Hasegawa
  • Takashi Yaeno
  • Koh Iba
  • Ryo Tabata
  • Kokoro Hayashi
  • Chojiro Kojima
  • Tsutomu Kawasaki
  • Ko Shimamoto
Conference paper

In this study, using yeast two-hybrid and in vitro binding assays, we found that the CA-OsRac1, but not the dominant negative form, interacted with the N-terminus of OsrbohB. The N-terminus contained two Ca2+-binding EF-hand motifs, was sufficient for OsRac1- OsrbohB interaction. Fluorescence resonance energy transfer microscopy showed that OsRac1 interacted with the N-terminus of OsrbohB predominantly in the GTP-bound form in vivo and the interaction was suppressed by cytosolic Ca2+ ions accumulation. Furthermore, in vitro NADPH oxidase activity assay also showed that GTP-bound OsRac1 enhanced NADPH oxidase activity and the activity was suppressed by Ca2+ ions.

Keywords

NADPH Oxidase Small GTPase NADPH Oxidase Activity Reactive Oxygen Species Signaling Dominant Negative Form 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer 2007

Authors and Affiliations

  • Hann Ling Wong
    • 1
  • Reinhard Pinontoan
    • 1
  • Kana Hasegawa
    • 1
  • Takashi Yaeno
    • 2
  • Koh Iba
    • 2
  • Ryo Tabata
    • 1
  • Kokoro Hayashi
    • 1
  • Chojiro Kojima
    • 1
  • Tsutomu Kawasaki
    • 1
  • Ko Shimamoto
    • 1
  1. 1.Nara Institute of Science and TechnologyJapan
  2. 2.Department of BiologyKyushu UniversityJapan

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