Thioredoxin-mediated reductive activation of a protein kinase for the regulatory phosphorylation of C4-form phosphoenolpyruvate carboxylase from maize

被引：41

作者：

Saze, H

Ueno, Y

Hisabori, T

Hayashi, H

Izui, K ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Agr, Div Appl Biosci, Sakyo Ku, Kyoto 6068502, Japan

[2] Tokyo Inst Technol, Resources Utilizat Res Lab, Midori Ku, Yokohama, Kanagawa 2268503, Japan

[3] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan

[4] Kyoto Univ, Grad Sch Biostudies, Lab Plant Physiol, Sakyo Ku, Kyoto 6068502, Japan

来源：

PLANT AND CELL PHYSIOLOGY | 2001年 / 42卷 / 12期

基金：

日本学术振兴会;

关键词：

phosphoenolpyruvate carboxylase kinase purification; redox-regulation; regulatory phosphorylation; thioredoxin; Zea mays;

D O I：

10.1093/pcp/pce182

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

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 M-r 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.

引用

页码：1295 / 1302

页数：8

共 45 条

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