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Analysis of RNA and enzymes of potential importance for regulation of 5-aminolevulinic acid synthesis in the protochlorophyllide accumulating barley mutant tigrina-d12

Hansson, Mats LU ; Gough, S. P.; Kannangara, C. G. and von Wettstein, D. (1997) In Plant Physiology and Biochemistry 35(11). p.827-836
Abstract
Dark-grown tigrina-d(12) mutants of barley (Hordeum vulgare L.) accumulate abnormally high amounts of the chlorophyll intermediate protochlorophyllide. In light dark cycles this leads to necrotic segments of the seedling leaves and lethality due to photodynamic damage by the excessive protochlorophyllide accumulated in the dark period. Upon inhibition of the early chlorophyll biosynthetic enzyme, 5-aminolevulinic acid (ALA)-dehydratase (EC 4.2.1.24) by levulinic acid, the mutant accumulates large amounts of ALA, while the wild type accumulates only a limited amount of ALA. Glutamyl-tRNA(Glu) synthetase (EC 6.1.1.17) mRNA was four times more abundant in the tigrina-d(12) mutant compared to the wild type, resulting in an up to 1.3 times... (More)
Dark-grown tigrina-d(12) mutants of barley (Hordeum vulgare L.) accumulate abnormally high amounts of the chlorophyll intermediate protochlorophyllide. In light dark cycles this leads to necrotic segments of the seedling leaves and lethality due to photodynamic damage by the excessive protochlorophyllide accumulated in the dark period. Upon inhibition of the early chlorophyll biosynthetic enzyme, 5-aminolevulinic acid (ALA)-dehydratase (EC 4.2.1.24) by levulinic acid, the mutant accumulates large amounts of ALA, while the wild type accumulates only a limited amount of ALA. Glutamyl-tRNA(Glu) synthetase (EC 6.1.1.17) mRNA was four times more abundant in the tigrina-d(12) mutant compared to the wild type, resulting in an up to 1.3 times higher enzymatic activity. In the dark grown mutant, glutamate 1-semialdehyde 2,1-aminotransferase (EC 5.4.3.8), ferrochelatase (EC 4.99.1.1), magnesium chelatase and the plastid encoded tRNA(Glu) was expressed to the same extent as in the dark grown wild type, while glutamyl-tRNA(Glu) reductase was expressed at a reduced level compared to the wild type. Since the abnormally high amounts of protochlorophyllide is based on an increased formation of ALA, the amount of ALA produced in the wild type in vivo must be sensed by one or several of the three ALA forming enzymes. The component of the sensing mechanism which is encoded by the tigrina-d gene has still to be identified. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Plant Physiology and Biochemistry
volume
35
issue
11
pages
827 - 836
publisher
Elsevier
external identifiers
  • scopus:0030727915
ISSN
1873-2690
language
English
LU publication?
no
id
b9b6ed2c-9642-49d3-9860-5ee504571b2e (old id 8001532)
date added to LUP
2015-10-01 11:00:19
date last changed
2017-01-01 07:02:37
@article{b9b6ed2c-9642-49d3-9860-5ee504571b2e,
  abstract     = {Dark-grown tigrina-d(12) mutants of barley (Hordeum vulgare L.) accumulate abnormally high amounts of the chlorophyll intermediate protochlorophyllide. In light dark cycles this leads to necrotic segments of the seedling leaves and lethality due to photodynamic damage by the excessive protochlorophyllide accumulated in the dark period. Upon inhibition of the early chlorophyll biosynthetic enzyme, 5-aminolevulinic acid (ALA)-dehydratase (EC 4.2.1.24) by levulinic acid, the mutant accumulates large amounts of ALA, while the wild type accumulates only a limited amount of ALA. Glutamyl-tRNA(Glu) synthetase (EC 6.1.1.17) mRNA was four times more abundant in the tigrina-d(12) mutant compared to the wild type, resulting in an up to 1.3 times higher enzymatic activity. In the dark grown mutant, glutamate 1-semialdehyde 2,1-aminotransferase (EC 5.4.3.8), ferrochelatase (EC 4.99.1.1), magnesium chelatase and the plastid encoded tRNA(Glu) was expressed to the same extent as in the dark grown wild type, while glutamyl-tRNA(Glu) reductase was expressed at a reduced level compared to the wild type. Since the abnormally high amounts of protochlorophyllide is based on an increased formation of ALA, the amount of ALA produced in the wild type in vivo must be sensed by one or several of the three ALA forming enzymes. The component of the sensing mechanism which is encoded by the tigrina-d gene has still to be identified.},
  author       = {Hansson, Mats and Gough, S. P. and Kannangara, C. G. and von Wettstein, D.},
  issn         = {1873-2690},
  language     = {eng},
  number       = {11},
  pages        = {827--836},
  publisher    = {Elsevier},
  series       = {Plant Physiology and Biochemistry},
  title        = {Analysis of RNA and enzymes of potential importance for regulation of 5-aminolevulinic acid synthesis in the protochlorophyllide accumulating barley mutant tigrina-d12},
  volume       = {35},
  year         = {1997},
}