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Plant and Cell Physiology, 2004, Vol. 45, No. 1 18-27
© 2004 Oxford University Press

Rapid Paper

Target Proteins of the Cytosolic Thioredoxins in Arabidopsis thaliana

Daisuke Yamazaki1,5, Ken Motohashi1,2,5, Takeshi Kasama3, Yukichi Hara4 and Toru Hisabori1,2,6

1 Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama, 226-8503 Japan
2 ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Agency (JST), 5800-3 Nagatsuta-cho, Midori-ku, Yokohama, 226-0026 Japan
3 Instrumental Analysis Research Center for Life Science, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8510 Japan
4 Department of Biochemistry and Biophysics, Graduate School of Health Sciences, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo, 113-8519 Japan

Possible target proteins of cytosolic thioredoxin in higher plants have been investigated in the cell lysate of dark-grown Arabidopsis thaliana whole tissues. We immobilized a mutant of cytosolic thioredoxin, in which an internal cysteine at the active site was substituted with serine, on CNBr activated resin, and used the resin for the thioredoxin-affinity chromatography. By using this resin, the target proteins for thioredoxin in the higher plant cytosol were efficiently acquired. The obtained proteins were separated by two-dimensional gel electrophoresis and analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Thus we have identified proteins of the anti-oxidative stress system proteins (ascorbate peroxidase, germin-like protein, and monomeric type II peroxiredoxin), proteins involved in protein biosynthesis (elongation factor-2 and eukaryotic translation initiation factor 4A), proteins involved in protein degradation (the regulatory subunit of 26S proteasome), and several metabolic enzymes (alcohol dehydrogenase, fructose 1,6-bis phosphate aldolase-like protein, cytosolic glyceraldehyde 3-phosphate dehydrogenase, cytosolic malate dehydrogenase, and vitamin B12-independent methionine synthase) together with some chloroplast proteins (chaperonin 60-{alpha} and 60-ß, heat shock protein 70, and glutamine synthase). The results in this study and recent proteomics studies on the target proteins of chloroplast thioredoxin indicate the versatility and the physiological significance of thioredoxin as reductant in plant cell.

5 D.Y. and K.M. contributed equally to this work.

6 Corresponding author: E-mail, thisabor{at}res.titech.ac.jp; Fax, +81-45-924-5277.


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