Reduced chlorophyll biosynthesis in heterozygous barley magnesium chelatase mutants
(2014) In Plant Physiology and Biochemistry 78. p.10-14- Abstract
- Chlorophyll biosynthesis is initiated by magnesium chelatase, an enzyme composed of three proteins, which catalyzes the insertion of Mg2+ into protoporphyrin IX to produce Mg-protoporphyrin IX. In barley (Hordeum vulgare L.) the three proteins are encoded by Xantha-f, Xantha-g and Xantha-h. Two of the gene products, XanH and XanG, belong to the structurally conserved family of AAA+ proteins (ATPases associated with various cellular activities) and form a complex involving six subunits of each protein. The complex functions as an ATP-fueled motor of the magnesium chelatase that uses XanF as substrate, which is the catalytic subunit responsible for the insertion of Mg2+ into protoporphyrin IX. Previous studies have shown that semi-dominant... (More)
- Chlorophyll biosynthesis is initiated by magnesium chelatase, an enzyme composed of three proteins, which catalyzes the insertion of Mg2+ into protoporphyrin IX to produce Mg-protoporphyrin IX. In barley (Hordeum vulgare L.) the three proteins are encoded by Xantha-f, Xantha-g and Xantha-h. Two of the gene products, XanH and XanG, belong to the structurally conserved family of AAA+ proteins (ATPases associated with various cellular activities) and form a complex involving six subunits of each protein. The complex functions as an ATP-fueled motor of the magnesium chelatase that uses XanF as substrate, which is the catalytic subunit responsible for the insertion of Mg2+ into protoporphyrin IX. Previous studies have shown that semi-dominant Xantha-h mutations result in non-functional XanH subunits that participate in the formation of inactive AAA complexes. In the present study, we identify severe mutations in the barley mutants xantha-h.38, -h.56 and -h.57. A truncated form of the protein is seen in xantha-h.38, whereas no XanH is detected in xantha-h.56 and -h.57. Heterozygous mutants show a reduction in chlorophyll content by 14-18% suggesting a slight semi-dominance of xantha-h.38, -h.56 and -h.57, which otherwise have been regarded as recessive mutations (Less)
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https://lup.lub.lu.se/record/7758727
- author
- Braumann, Ilka ; Stein, Nils and Hansson, Mats LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Plant Physiology and Biochemistry
- volume
- 78
- pages
- 10 - 14
- publisher
- Elsevier
- external identifiers
-
- scopus:84897670628
- pmid:24607574
- ISSN
- 1873-2690
- DOI
- 10.1016/j.plaphy.2014.02.004
- language
- English
- LU publication?
- yes
- id
- 93325d4b-a40f-4e25-a76a-38bae068e71a (old id 7758727)
- date added to LUP
- 2016-04-01 13:02:45
- date last changed
- 2025-04-04 13:53:29
@article{93325d4b-a40f-4e25-a76a-38bae068e71a,
abstract = {{Chlorophyll biosynthesis is initiated by magnesium chelatase, an enzyme composed of three proteins, which catalyzes the insertion of Mg2+ into protoporphyrin IX to produce Mg-protoporphyrin IX. In barley (Hordeum vulgare L.) the three proteins are encoded by Xantha-f, Xantha-g and Xantha-h. Two of the gene products, XanH and XanG, belong to the structurally conserved family of AAA+ proteins (ATPases associated with various cellular activities) and form a complex involving six subunits of each protein. The complex functions as an ATP-fueled motor of the magnesium chelatase that uses XanF as substrate, which is the catalytic subunit responsible for the insertion of Mg2+ into protoporphyrin IX. Previous studies have shown that semi-dominant Xantha-h mutations result in non-functional XanH subunits that participate in the formation of inactive AAA complexes. In the present study, we identify severe mutations in the barley mutants xantha-h.38, -h.56 and -h.57. A truncated form of the protein is seen in xantha-h.38, whereas no XanH is detected in xantha-h.56 and -h.57. Heterozygous mutants show a reduction in chlorophyll content by 14-18% suggesting a slight semi-dominance of xantha-h.38, -h.56 and -h.57, which otherwise have been regarded as recessive mutations}},
author = {{Braumann, Ilka and Stein, Nils and Hansson, Mats}},
issn = {{1873-2690}},
language = {{eng}},
pages = {{10--14}},
publisher = {{Elsevier}},
series = {{Plant Physiology and Biochemistry}},
title = {{Reduced chlorophyll biosynthesis in heterozygous barley magnesium chelatase mutants}},
url = {{http://dx.doi.org/10.1016/j.plaphy.2014.02.004}},
doi = {{10.1016/j.plaphy.2014.02.004}},
volume = {{78}},
year = {{2014}},
}