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JXB Advance Access originally published online on March 2, 2006
Journal of Experimental Botany 2006 57(5):1109-1118; doi:10.1093/jxb/erj134
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© The Author [2006]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

An accurate and reproducible method for proteome profiling of the effects of salt stress in the rice leaf lamina

Robert Parker1,*, Timothy J. Flowers1, Anthony L. Moore1 and Nicholas V. J. Harpham2

1School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK
2University of Sussex Proteomics Facility, University of Sussex, Trafford Centre, Falmer, Brighton BN1 9SB, UK

* To whom correspondence should be addressed. E-mail: r.parker{at}sussex.ac.uk

Proteomic analysis of any biological system by two-dimensional gel electrophoresis (2-DE) requires high resolution and high reproducibility. The results presented here demonstrate the reproducible and accurate separation of rice (Oryza sativa L.) proteins using improved procedures for high resolution 2-DE, which were adapted for the separation of rice lamina proteins. Validation of this system was achieved by measuring the effects of sample preparation and biological variation on the coefficient of variation (CV) for replicate spots. The majority of experimental variation was shown to be introduced by the 2-DE technique (CV 0.26). Analysis of biological variation indicated that approximately 93–95% of spots were within a CV of 0.7. This provided a threshold value from which valid differences in expression between experimental groups could be screened. This system was then utilized for the proteomic analysis of short- and long-term salt-stress-responsive proteins in the rice leaf lamina. Analysis resulted in the separation of approximately 2500 protein species of which 32 were observed to be significantly regulated by salinity; so far 11 of these proteins have been identified by tandem mass spectrometry. An increase in eight proteins, including RuBisCO activase and ferritin, occurred by 24 h of exposure to sodium chloride (50 mM) and continued to increase during the following 6 d. Only one protein, a putative phosphoglycerate kinase, was found to increase in expression within 24 h and did not increase over a longer period of exposure to salt. There were also proteins that showed no change 24 h after exposure to salt, but had increased (superoxide dismutase) or decreased (S-adenosyl-L-methionine synthetase) after 7 d salt treatment.

Key words: Experimental error, Oryza sativa, proteomics, rice, salinity, salt stress


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