Proteomic analysis of rice leaf sheath during drought stress

J Proteome Res. 2006 Feb;5(2):396-403. doi: 10.1021/pr050291g.

Abstract

Drought is one of the most severe limitations on the productivity of rainfed lowland and upland rice. To investigate the initial response of rice to drought stress, changes in protein expression were analyzed using a proteomic approach. Two-week-old rice seedlings were exposed to drought conditions from 2 to 6 days, and proteins were extracted from leaf sheaths, separated by two-dimensional polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue. After drought stress for 2 to 6 days, 10 proteins increased in abundance and the level of 2 proteins decreased. The functional categories of these proteins were identified as defense, energy, metabolism, cell structure, and signal transduction. In addition to drought stress, accumulations of protein were analyzed under several different stress conditions. The levels of an actin depolymerizing factor, a light harvesting complex chain II, a superoxidase dismutase and a salt-induced protein were changed by drought and osmotic stresses, but not cold or salt stresses, or abscisic acid treatment. The effect of drought stress on protein in the leaf sheaths of drought-tolerant rice cultivar was also analyzed. The light harvesting complex chain II and the actin depolymerizing factor were present at high levels in a drought-tolerant rice cultivar before stress application. With drought stress, actin depolymerizing factor was expressed in leaf blades, leaf sheaths, and roots. These results suggest that actin depolymerizing factor is one of the target proteins induced by drought stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Disasters*
  • Electrophoresis, Gel, Two-Dimensional
  • Gene Expression Regulation, Plant
  • Oryza / genetics
  • Oryza / physiology*
  • Peptide Mapping
  • Plant Leaves / metabolism*
  • Plant Proteins / metabolism*
  • Plants, Genetically Modified
  • Seedlings / metabolism
  • Sequence Analysis, Protein

Substances

  • Plant Proteins