Characterization of a calcium-dependent protein kinase of tobacco leaves that is associated with the plasma membrane and is inducible by sucrose

被引：34

作者：

Iwata, Y ^{[1
]}

Kuriyama, M

Nakakita, H

Kojima, H

Ohto, M

Nakamura, K

机构：

[1] Nagoya Univ, Biochem Lab, Grad Sch Bioagr Sci, Nagoya, Aichi 4648601, Japan

[2] Natl Inst Basic Biol, Div Dev Biol, Okazaki, Aichi 4448585, Japan

来源：

PLANT AND CELL PHYSIOLOGY | 1998年 / 39卷 / 11期

关键词：

CDPK; plasma membrane; protein kinase; sugar-induced gene expression; tobacco (Nicotiana tabacum);

D O I：

10.1093/oxfordjournals.pcp.a029318

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

The plasma membrane fraction from leaves of tobacco contains a 54-kDa protein with autophosphorylation activity, and the level of this protein increases after feeding of leaves with sucrose [Ohto and Nakamura (1995) Plant Physiol. 109: 973]. The 54-kDa autophosphorylation protein could not be released from the plasma membrane by treatment with salt or alkali but could be efficiently solubilized by 1% sodium deoxycholate (NaDOC). Ion-exchange chromatography of the NaDOC-solubilized proteins in the presence of octylglucoside separated the 54-kDa autophosphorylation protein into three peaks. The autophosphorylation activity of the 54-kDa protein in peaks I and II increased after feeding of leaves with sucrose. The 54-kDa protein in the peak II fraction was enriched about 125-fold starting from the microsomal membrane fraction. The 54-kDa protein in this fraction phosphorylated histone IIIS in a calcium-dependent manner and cross-reacted with an antibody against a calcium-dependent protein kinase (CDPK) of Arabidopsis thaliana. These results suggest that the 54-kDa protein in the peak II fraction is a novel isoform of CDPK which is associated with the plasma membrane and is inducible by sucrose.

引用

页码：1176 / 1183

页数：8

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