Identification of gibberellin acid-responsive proteins in rice leaf sheath using proteomics

Front Biosci (Landmark Ed). 2010 Jun 1;15:826-39. doi: 10.2741/3648.


The phytohormone gibberellin acid (GA) controls many aspects of plant development. In this study, we identified proteins that are differentially expressed between the rice (Oryza sativa L.) GA-deficient cultivar, Aijiaonante, and its parental line, Nante. Proteins were extracted from rice leaf sheath and examined by 2DGE. Among more than 1200 protein spots reproducibly detected on each gel, 29 were found to be highly up-regulated by GAs in Nante, and 6 were down-regulated by GAs in Aijiaonante. These 35 proteins were identified by MALDI-TOF MS and were classified into three groups based on their putative function in metabolism, stress/defense processes and signal transduction. These data suggest that metabolic pathways are the main target of regulation by GAs during rice development. Our results provide new information about the involvement of GAs in rice development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • Electrophoresis, Gel, Two-Dimensional
  • Gibberellins / metabolism
  • Gibberellins / pharmacology*
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism
  • Mutation
  • Oryza / drug effects*
  • Oryza / genetics
  • Oryza / metabolism
  • Plant Growth Regulators / pharmacology
  • Plant Leaves / drug effects*
  • Plant Leaves / genetics
  • Plant Leaves / metabolism
  • Plant Proteins / analysis*
  • Plant Proteins / genetics
  • Proteome / analysis
  • Proteome / genetics
  • Proteomics / methods*
  • Sequence Analysis, DNA
  • Sequence Deletion
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization


  • DNA, Complementary
  • Gibberellins
  • Plant Growth Regulators
  • Plant Proteins
  • Proteome
  • Mixed Function Oxygenases
  • gibberellin, 2-oxoglutarate-oxygen oxidoreductase (20-hydroxylating, oxidizing)