Proteomic analysis of rice leaves during drought stress and recovery

Gh. Hosseini Salekdeh, Joel Siopongco, Leonard J. Wade, Behzad Ghareyazie, John Bennett*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

361 Citations (Scopus)

Abstract

Three-week old plants of rice (Oryza sativa L. cv CT9993 and cv IR62266) developed gradual water stress over 23 days of transpiration without watering, during which period the mid-day leaf water potential declined to ∼-2.4 MPa, compared with ∼-1.0 MPa in well-watered controls. More than 1000 protein spots that were detected in leaf extracts by proteomic analysis showed reproducible abundance within replications. Of these proteins, 42 spots showed a significant change in abundance under stress, with 27 of them exhibiting a different response pattern in the two cultivars. However, only one protein (chloroplast Cu-Zn superoxide dismutase) changed significantly in opposite directions in the two cultivars in response to drought. The most common difference was for proteins to be up-regulated by drought in CT9993 and unaffected in IR62266; or down-regulated by drought in IR62266 and unaffected in CT9993. By 10 days after rewatering, all proteins had returned completely or largely to the abundance of the well-watered control. Mass spectrometry helped to identify 16 of the drought-responsive proteins, including an actin depolymerizing factor, which was one of three proteins detectable under stress in both cultivars but undetectable in well-watered plants or in plants 10 days after rewatering. The most abundant protein up-regulated by drought in CT9993 and IR62266 was identified only after cloning of the corresponding cDNA. It was found to be an S-like RNase homologue but it lacked the two active site histidines required for RNase activity. Four novel drought-responsive mechanisms were revealed by this work: up-regulation of S-like RNase homologue, actin depolymerizing factor and rubisco activase, and down-regulation of isoflavone reductase-like protein.

Original languageEnglish
Pages (from-to)1131-1145
Number of pages15
JournalProteomics
Volume2
Issue number9
DOIs
Publication statusPublished - 1 Sep 2002
Externally publishedYes

Keywords

  • Actin depolymerizing factor
  • Mass spectrometry
  • Rubisco activase
  • S-like ribonuclease

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