ArticleThe Plant cell2006
Recessiveness and dominance in barley mutants deficient in Mg-chelatase subunit D, an AAA protein involved in chlorophyll biosynthesis.
Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 56 citations in OpenAlex.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Identification of a locus on Agropyron cristatum chromosome 6P that interacts with wheat genes to produce yellow-green leaves.BMC plant biology · 2025Article
- Yellow barley xan-m mutants are deficient in the motor unit SECA1 of the SEC1 translocase system.Planta · 2025Article
- Barley young leaf chlorina, a putative pentatricopeptide repeat gene, is essential for chloroplast development in young leaves.Plant molecular biology · 2025Article
- Exploring the interplay between angiosperm chlorophyll metabolism and environmental factors.Planta · 2024Review
- Post-translational regulation of metabolic checkpoints in plant tetrapyrrole biosynthesis.Journal of experimental botany · 2022Review
- SlRCM1, which encodes tomato Lutescent1, is required for chlorophyll synthesis and chloroplast development in fruits.Horticulture research · 2021Article
- Insights into the structure and function of the rate-limiting enzyme of chlorophyll degradation through analysis of a bacterial Mg-dechelatase homolog.Computational and structural biotechnology journal · 2021Article
- Mutation of theFrontiers in plant science · 2021Article
- Heterologous Expression of the Barley (Hordeum vulgare L.) Xantha-f, -g and -h Genes that Encode Magnesium Chelatase Subunits.The protein journal · 2020Article
- Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis.Protein science : a publication of the Protein Society · 2020Article
- Post-translational coordination of chlorophyll biosynthesis and breakdown by BCMs maintains chlorophyll homeostasis during leaf development.Nature communications · 2020Article
- The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase.The Biochemical journal · 2019Article
- Mapped clone and functional analysis of leaf-color gene Ygl7 in a rice hybrid (Oryza sativa L. ssp. indica).PloS one · 2014Article
- The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.The Journal of biological chemistry · 2013Article
- Catalytic turnover triggers exchange of subunits of the magnesium chelatase AAA+ motor unit.The Journal of biological chemistry · 2013Article
- Chlorophyll biosynthesis gene evolution indicates photosystem gene duplication, not photosystem merger, at the origin of oxygenic photosynthesis.Genome biology and evolution · 2013Article
- The barley magnesium chelatase 150-kd subunit is not an abscisic acid receptor.Plant physiology · 2009Article
- Recent overview of the Mg branch of the tetrapyrrole biosynthesis leading to chlorophylls.Photosynthesis research · 2008Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mg-chelatase catalyzes the insertion of Mg2+ into protoporphyrin IX at the first committed step of the chlorophyll biosynthetic pathway. It consists of three subunits: I, D, and H. The I subunit belongs to the AAA protein superfamily (ATPases associated with various cellular activities) that is known to form hexameric ring structures in an ATP-dependant fashion. Dominant mutations in the I subunit revealed that it functions in a cooperative manner. We demonstrated that the D subunit forms ATP-independent oligomeric structures and should also be classified as an AAA protein. Furthermore, we addressed the question of cooperativity of the D subunit with barley (Hordeum vulgare) mutant analyses. The recessive behavior in vivo was explained by the absence of mutant proteins in the barley cell. Analogous mutations in Rhodobacter capsulatus and the resulting D proteins were studied in vitro. Mixtures of wild-type and mutant R. capsulatus D subunits showed a lower activity compared with wild-type subunits alone. Thus, the mutant D subunits displayed dominant behavior in vitro, revealing cooperativity between the D subunits in the oligomeric state. We propose a model where the D oligomer forms a platform for the stepwise assembly of the I subunits. The cooperative behavior suggests that the D oligomer takes an active part in the conformational dynamics between the subunits of the enzyme.
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