First published online December 29, 2008; 10.1105/tpc.108.063263
The Plant Cell 20:3210-3226 (2008)
© 2008 American Society of Plant Biologists
OPEN ACCESS ARTICLE
Functional Proteomics of Arabidopsis thaliana Guard Cells Uncovers New Stomatal Signaling Pathways[W],[OA]
Zhixin Zhaoa,
Wei Zhanga,
Bruce A. Stanleyb and
Sarah M. Assmanna,1
a Biology Department, Penn State University, University Park, Pennsylvania 16802
b Section of Research Resources, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033
1 Address correspondence to sma3{at}psu.edu.
We isolated a total of 3 x 108 guard cell protoplasts from 22,000 Arabidopsis thaliana plants and identified 1734 unique proteins using three complementary proteomic methods: protein spot identification from broad and narrow pH range two-dimensional (2D) gels, and 2D liquid chromatography–matrix assisted laser desorption/ionization multidimensional protein identification technology. This extensive single-cell-type proteome includes 336 proteins not previously represented in transcriptome analyses of guard cells and 52 proteins classified as signaling proteins by Gene Ontology analysis, of which only two have been previously assessed in the context of guard cell function. THIOGLUCOSIDE GLUCOHYDROLASE1 (TGG1), a myrosinase that catalyzes the production of toxic isothiocyanates from glucosinolates, showed striking abundance in the guard cell proteome. tgg1 mutants were hyposensitive to abscisic acid (ABA) inhibition of guard cell inward K+ channels and stomatal opening, revealing that the glucosinolate-myrosinase system, previously identified as a defense against biotic invaders, is required for key ABA responses of guard cells. Our results also suggest a mechanism whereby exposure to abiotic stresses may enhance plant defense against subsequent biotic stressors and exemplify how enhanced knowledge of the signaling networks of a specific cell type can be gained by proteomics approaches.
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