Plant and Cell Physiology, 2004, Vol. 45, No. 6 672-683
© 2004 Oxford University Press
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Isolation of Intact Vacuoles and Proteomic Analysis of Tonoplast from Suspension-Cultured Cells of Arabidopsis thaliana
1 Department of Biological Science, Faculty of Science, Nara-Women’s University, Nara, 630-8506 Japan
2 Plant Research Group, Research Institute of Innovative Technology for the Earth, 9-2 Kizugawadai, Kizu-cho, Soraku-gun, Kyoto, 619-0292 Japan
3 Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation (JST), Chuou-ku, Tokyo, 113-0027 Japan
4 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan
5 Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502 Japan
6 Department of Biology, Faculty of Science, Kyushu University, Ropponmatsu, Fukuoka, 810-8560 Japan
7 Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara, 630-0101 Japan
A large number of proteins in the tonoplast, including pumps, carriers, ion channels and receptors support the various functions of the plant vacuole. To date, few proteins involved in these activities have been identified at the molecular level. In this study, proteomic analysis was used to identify new tonoplast proteins. A primary requirement of any organelle analysis by proteomics is that the purity of the isolated organelle needs to be high. Using suspension-cultured Arabidopsis cells (Arabidopsis Col-0 cell suspension), a method was developed for the isolation of intact highly purified vacuoles. No plasma membrane proteins were detected in Western blots of the isolated vacuole fraction, and only a few proteins from the Golgi and endoplasmic reticulum. The proteomic analysis of the purified tonoplast involved fractionation of the proteins by SDS-PAGE and analysis by LC-MS/MS. Using this approach, it was possible to identify 163 proteins. These included well-characterized tonoplast proteins such as V-type H+-ATPases and V-type H+-PPases, and others with functions reasonably expected to be related to the tonoplast. There were also a number of proteins for which a function has not yet been deduced.
8 Present address: Department of Biology, Faculty of Science, Kobe University, 1-1, Rokkodai, Nada-ku, Kobe, 657-8501 Japan.
9 Corresponding author: E-mail, mimura{at}kobe-u.ac.jp, Fax, +81-78-803-5708.
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