The barley magnesium chelatase 150-kd subunit is not an abscisic acid receptor
(2009) In Plant Physiology 150(1). p.157-166- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8001571
- author
- Muller, A. H. and Hansson, Mats LU
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Plant Stomata/drug effects, Plant Proteins/genetics/*metabolism/physiology, Plant Growth Regulators/*metabolism, Mutation, Molecular Sequence Data, Lyases/genetics/*metabolism/physiology, Hordeum/drug effects/*enzymology/genetics, Germination, Abscisic Acid/*metabolism/pharmacology, Amino Acid Sequence, Protein Subunits/genetics/metabolism/physiology, Receptors, Cell Surface/genetics/*metabolism, Recombinant Fusion Proteins/metabolism, Sequence Alignment
- in
- Plant Physiology
- volume
- 150
- issue
- 1
- pages
- 157 - 166
- publisher
- American Society of Plant Biologists
- external identifiers
-
- scopus:66149104005
- ISSN
- 1532-2548
- DOI
- 10.1104/pp.109.135277
- language
- English
- LU publication?
- no
- additional info
- 1
- id
- efa10e26-d944-4393-bdb5-eca858c96baf (old id 8001571)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/19176716
- date added to LUP
- 2016-04-01 11:43:39
- date last changed
- 2022-01-26 17:17:44
@article{efa10e26-d944-4393-bdb5-eca858c96baf,
abstract = {{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.}},
author = {{Muller, A. H. and Hansson, Mats}},
issn = {{1532-2548}},
keywords = {{Plant Stomata/drug effects; Plant Proteins/genetics/*metabolism/physiology; Plant Growth Regulators/*metabolism; Mutation; Molecular Sequence Data; Lyases/genetics/*metabolism/physiology; Hordeum/drug effects/*enzymology/genetics; Germination; Abscisic Acid/*metabolism/pharmacology; Amino Acid Sequence; Protein Subunits/genetics/metabolism/physiology; Receptors; Cell Surface/genetics/*metabolism; Recombinant Fusion Proteins/metabolism; Sequence Alignment}},
language = {{eng}},
number = {{1}},
pages = {{157--166}},
publisher = {{American Society of Plant Biologists}},
series = {{Plant Physiology}},
title = {{The barley magnesium chelatase 150-kd subunit is not an abscisic acid receptor}},
url = {{http://dx.doi.org/10.1104/pp.109.135277}},
doi = {{10.1104/pp.109.135277}},
volume = {{150}},
year = {{2009}},
}