The Barley Magnesium Chelatase 150-kD Subunit Is Not an Abscisic Acid Receptor

被引：74

作者：

Muller, Andre H. ^{[1
]}

Hansson, Mats ^{[1
]}

机构：

[1] Carlsberg Lab, DK-2500 Copenhagen, Denmark

来源：

PLANT PHYSIOLOGY | 2009年 / 150卷 / 01期

关键词：

MG-PROTOPORPHYRIN-IX; BINDING PROTEIN; H-SUBUNIT; CHLOROPHYLL BIOSYNTHESIS; MUTANTS DEFICIENT; ATPASE ACTIVITY; IN-VIVO; ARABIDOPSIS; NUCLEUS; CHLOROPLAST;

D O I：

10.1104/pp.109.135277

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Magnesium chelatase is the first unique enzyme of the chlorophyll biosynthetic pathway. It is composed of three gene products of which the largest is 150 kD. This protein was recently identified as an abscisic acid receptor in Arabidopsis (Arabidopsis thaliana). We have evaluated whether the barley (Hordeum vulgare) magnesium chelatase large subunit, XanF, could be a receptor for the phytohormone. The study involved analysis of recombinant magnesium chelatase protein as well as several induced chlorophyll-deficient magnesium chelatase mutants with defects identified at the gene and protein levels. Abscisic acid had no effect on magnesium chelatase activity and binding to the barley 150-kD protein could not be shown. Magnesium chelatase mutants showed a wild-type response in respect to postgermination growth and stomatal aperture. Our results question the function of the large magnesium chelatase subunit as an abscisic acid receptor.

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收藏

页码：157 / 166

页数：10

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