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Mg-chelatase I subunit 1 and Mg-protoporphyrin IX methyltransferase affect the stomatal aperture in Arabidopsis thaliana.

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To elucidate the molecular mechanisms of stomatal opening and closure, we performed a genetic screen using infrared thermography to isolate stomatal aperture mutants. We identified a mutant designated low temperature with open-stomata 1 (lost1), which exhibited reduced leaf temperature, wider

The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes.

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Chlorophyll biosynthesis requires a metabolic dialog between the chloroplast envelope and thylakoids where biosynthetic activities are localized. Here, we report the first plant S-adenosyl-l-methionine:Mg-protoporphyrin IX methyltransferase (MgP(IX)MT) sequence identified in the Arabidopsis genome

Xantha-l encodes a membrane subunit of the aerobic Mg-protoporphyrin IX monomethyl ester cyclase involved in chlorophyll biosynthesis.

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Chlorophyll biosynthesis is a process involving approximately 20 different enzymatic steps. Half of these steps are common to the biosynthesis of other tetrapyrroles, such as heme. One of the least understood enzymatic steps is formation of the isocyclic ring, which is a characteristic feature of

Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant.

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Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme. It is located in the mitochondria in all eukaryotes and is also found in plastids in plants. Although it has been purified from animals and microorganisms, and genes for it isolated and characterized,

Molecular characterization and primary functional analysis of PeMPEC, a magnesium-protoporphyrin IX monomethyl ester cyclase gene of bamboo (Phyllostachys edulis).

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CONCLUSIONS A homologous gene of MPEC from Phyllostachys edulis was isolated and characterized. Its overexpression in Arabidopsis thaliana increased chlorophyll concentration and photosynthesis efficiency, indicating it is involved in chlorophyll biosynthesis. Magnesium-protoporphyrin IX monomethyl

Characterization of the haem oxygenase protein family in Arabidopsis thaliana reveals a diversity of functions.

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HOs (haem oxygenases) catalyse the oxidative cleavage of haem to BV (biliverdin), iron and carbon monoxide. In plants, the product of the reaction is BV IXalpha, the precursor of the PHY (phytochrome) chromophore and is thus essential for proper photomorphogenesis. Arabidopsis thaliana contains one

[Evolution aspects of intraspecific polymorphysm of Arabidopsis thaliana genes coding subunit I of Mg-chelatase complex].

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Intraspecific polymorphism in the CHLI 2 gene, coding subunit I of Mg-chelatase complex that forms Mg-protoporphyrin IX was investigated in 19 ecotypes of Arabidopsis thaliana. Sequence divergence by 35 nucleotides was found; 12 of them result into amino acid change in third exon where functional

Light signalling pathways regulating the Mg-chelatase branchpoint of chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.

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Precise regulation of tetrapyrrole synthesis is critical for plant survival when seedlings first emerge into the light. At this time there is a massive increase in demand for chlorophyll to drive the assembly of the photosynthetic apparatus. To understand how this demand is met we have followed the

Functional characterization of the two ferrochelatases in Arabidopsis thaliana.

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The enzyme ferrochelatase catalyses the formation of protoheme by inserting Fe(2+) into protoporphyrin IX. Although most organisms express only one ferrochelatase, all land plants analysed so far possess at least two ferrochelatase proteins. Analysis of publicly available expression data suggests

The CHLI1 subunit of Arabidopsis thaliana magnesium chelatase is a target protein of the chloroplast thioredoxin.

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Insertion of magnesium into protoporphyrin IX by magnesium chelatase is a key step in the chlorophyll biosynthetic pathway, which takes place in plant chloroplasts. ATP hydrolysis by the CHLI subunit of magnesium chelatase is an essential component of this reaction, and the activity of this enzyme

Isolation and characterisation of tobacco (Nicotiana tabacum) cDNA clones encoding proteins involved in magnesium chelation into protoporphyrin IX.

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We have identified cDNA clones encoding the two Mg chelatase subunits CHL I and CHL H from tobacco (Nicotiana tabacum) by screening a cDNA library with homologous cDNA fragments from Arabidopsis thaliana. A full-length Chl I cDNA clone encodes a peptide with 426 amino acids. The entire cDNA sequence

Characterization of cytosolic tetrapyrrole-binding proteins in Arabidopsis thaliana.

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In plant cells, tetrapyrroles are synthesized in plastids and distributed to numerous organelles to function in various vital activities. However, molecular mechanisms of tetrapyrroles trafficking in plant cells are poorly understood. In animal cells, experimental evidence suggests that the

The mitochondrion--an organelle commonly involved in programmed cell death in Arabidopsis thaliana.

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Plant cells undergoing programmed cell death (PCD) at late stages typically show chromatin condensation and endonucleolytic cleavage prior to obvious membrane or organelle ultrastructural changes. To investigate possible early PCD-associated events, we used microscopic observations and flow

The light stress-induced protein ELIP2 is a regulator of chlorophyll synthesis in Arabidopsis thaliana.

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The early light-induced proteins (ELIPs) belong to the multigenic family of pigment-binding light-harvesting complexes. ELIPs accumulate transiently and are believed to play a protective role in plants exposed to high levels of light. Constitutive expression of the ELIP2 gene in Arabidopsis resulted

A novel Arabidopsis thaliana protein is a functional peripheral-type benzodiazepine receptor.

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A key element in the regulation of mammalian steroid biosynthesis is the 18 kDa peripheral-type benzodiazepine receptor (PBR), which mediates mitochondrial cholesterol import. PBR also possess an affinity to the tetrapyrrole metabolite protoporphyrin. The bacterial homolog to the mammalian PBR, the

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