Reduced chlorophyll biosynthesis in heterozygous barley magnesium chelatase mutants

Copyright © 2014 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 78(2014) vom: 01. Mai, Seite 10-4
1. Verfasser: Braumann, Ilka (VerfasserIn)
Weitere Verfasser: Stein, Nils, Hansson, Mats
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't AAA BchI ChlI Hordeum vulgare Mg-chelatase Plant Proteins Protein Subunits Chlorophyll mehr... 1406-65-1 Lyases EC 4.- magnesium chelatase EC 4.99.1-
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520 |a Copyright © 2014 Elsevier Masson SAS. All rights reserved. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a AAA 
650 4 |a BchI 
650 4 |a ChlI 
650 4 |a Hordeum vulgare 
650 4 |a Mg-chelatase 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Protein Subunits  |2 NLM 
650 7 |a Chlorophyll  |2 NLM 
650 7 |a 1406-65-1  |2 NLM 
650 7 |a Lyases  |2 NLM 
650 7 |a EC 4.-  |2 NLM 
650 7 |a magnesium chelatase  |2 NLM 
650 7 |a EC 4.99.1-  |2 NLM 
700 1 |a Stein, Nils  |e verfasserin  |4 aut 
700 1 |a Hansson, Mats  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 78(2014) vom: 01. Mai, Seite 10-4  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnas 
773 1 8 |g volume:78  |g year:2014  |g day:01  |g month:05  |g pages:10-4 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2014.02.004  |3 Volltext 
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