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Plant and Cell Physiology, 2001, Vol. 42, No. 12 1295-1302
© 2001 Oxford University Press

Thioredoxin-Mediated Reductive Activation of a Protein Kinase for the Regulatory Phosphorylation of C4-form Phosphoenolpyruvate Carboxylase from Maize

Hidetoshi Saze1,5,6, Yoshihisa Ueno1,5,7, Toru Hisabori2, Hiroaki Hayashi3 and Katsura Izui1,4,8

1 Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502 Japan 2 Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta 4259, Midori-Ku, Yokohama, 226-8503 Japan 3 Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-8657 Japan 4 Laboratory of Plant Physiology, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto, 606-8502 Japan

The activity of phosphoenolpyruvate carboxylase (PEPC, EC4.1.1.31) for the C4 photosynthesis is known to be regulated mainly in response to light/dark transitions through reversible phosphorylation by a specific protein kinase (PK). PEPC-PK with an Mr of 30 kDa was purified about 1.4 million-fold to homogeneity from maize leaves and characterized. The purified PEPC-PK was readily inactivated under mild oxidative conditions, but the activity could be recovered by dithiothreitol (DTT). The recovery by DTT was strongly accelerated by thioredoxin (Trx) from E. coli. Trxs of plant origin such as Trx-m from spinach chloroplast and Trx-h from rice cytoplasm were also effective. These results suggest the possibility of PEPC-PK being redox-regulated via Trx in vivo.

5 These authors made equal contribution to this work.

6 Present address: Friedrich Miescher Institute, Basel, Switzerland.

7 Present address: Division of Biological Science, Graduate School of Science, Nagoya, University, Chikusa-ku, Nagoya, 464-8602 Japan.

8 Corresponding author: E-mail, izui@kais.kyoto-u.ac.jp; Fax, +81-75-753-6470.


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