Identification of Green-Revertible Yellow 3 (GRY3), encoding a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase involved in chlorophyll synthesis under high temperature and high light in rice
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Abstract:
Chlorophyll, a green pigment in photosynthetic organisms, is generated by two distinct biochemical pathways, the tetrapyrrole biosynthetic pathway (TBP) and the methylerythritol 4-phosphate (MEP) pathway. MEP is one of the pathways for isoprenoid synthesis in plants, with 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR) catalyzing its last step. In this study, we isolated a green-revertible yellow leaf mutant gry3 in rice and cloned the GRY3 gene, which encodes a HDR participating in geranylgeranyl diphosphate (GGPP) biosynthesis in chloroplast. A complementation experiment confirmed that a missense mutation (C to T) in the fourth exon of LOC_Os03g52170 causes the gry3 phenotype. Under high temperature and high light, transcript and protein abundances of GRY3 were reduced in the gry3 mutant. Transcriptional expression of chlorophyll biosynthesis, chloroplast development, and genes involved in photosynthesis were also affected. Excessive reactive oxygen species accumulation, cell death, and photosynthetic proteins degradation were occurred in the mutant. The content of GGPP was reduced in gry3 compared with Nipponbare, resulting in a stoichiometric imbalance of tetrapyrrolic chlorophyll precursors. These results shed light on the response of chloroplast biogenesis and maintenance in plants to high-temperature and high-light stress.Keywords:
Protochlorophyllide
Tetrapyrrole
Protochlorophyllide
Tetrapyrrole
Etiolation
Protoporphyrin IX
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Protochlorophyllide
Tetrapyrrole
Uroporphyrinogen III decarboxylase
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The aurea (au) and yellow-green-2 (yg-2) mutants of tomato (Solanum lycopersicum L.) are unable to synthesize the linear tetrapyrrole chromophore of phytochrome, resulting in plants with a yellow-green phenotype. To understand the basis of this phenotype, we investigated the consequences of the au and yg-2 mutations on tetrapyrrole metabolism. Dark-grown seedlings of both mutants have reduced levels of protochlorophyllide (Pchlide) due to an inhibition of Pchlide synthesis. Feeding experiments with the tetrapyrrole precursor 5-aminolevulinic acid (ALA) demonstrate that the pathway between ALA and Pchlide is intact in au and yg-2 and suggest that the reduction in Pchlide is a result of the inhibition of ALA synthesis. This inhibition was independent of any deficiency in seed phytochrome, and experiments using an iron chelator to block heme synthesis demonstrated that both mutations inhibited the degradation of the physiologically active heme pool, suggesting that the reduction in Pchlide synthesis is a consequence of feedback inhibition by heme. We discuss the significance of these results in understanding the chlorophyll-deficient phenotype of the au and yg-2 mutants.
Tetrapyrrole
Protochlorophyllide
Phytochrome
Chromophore
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Summary Previous studies have established that the expression of mammalian biliverdin IXα reductase (BVR) in transgenic tobacco ( Nicotiana tabacum cv. Maryland Mammoth) resulted in the loss of photoregulatory activity of all phytochromes together with a pronounced chlorophyll deficiency. This study was undertaken to assess the contribution of BVR‐mediated alteration of tetrapyrrole metabolism to the observed phenotypes of BVR transgenic plants. BVR expression in dark‐grown plants led to the reduced accumulation of protochlorophyllide and transcripts for the two committed enzymes for 5‐aminolevulinic acid (ALA) synthesis despite the marked increased capacity for synthesis of ALA. Together with the observation that Mg‐porphyrin accumulation in dark‐grown seedlings treated with an iron chelator was unaffected by BVR expression, these results indicate that BVR diverts tetrapyrrole metabolism toward heme synthesis while also reducing heme levels to de‐repress ALA synthesis. By contrast with dark‐grown seedlings, light‐grown BVR plants showed a marked inhibition of ALA synthesis compared with wild‐type plants – a result that was correlated with the disappearance of the CHL I subunit of Mg‐chelatase and an increase in heme oxygenase protein levels. As transcript levels of all tetrapyrrole biosynthetic genes tested were not strongly affected by BVR expression, these results implicate misregulated tetrapyrrole metabolism to be a major mechanism for BVR‐dependent inhibition of chlorophyll biosynthesis in light‐grown plants.
Tetrapyrrole
Protochlorophyllide
Biliverdin reductase
Biliverdin
Phytochrome
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Chlorophyllides can be found in photosynthetic organisms. Generally, chlorophyllides have a-, b-, c-, d-, and f-type derivatives, and all chlorophyllides have a tetrapyrrole structure with a Mg ion at the center and a fifth isocyclic pentanone. Chlorophyllide a can be synthesized from protochlorophyllide a, divinyl chlorophyllide a, or chlorophyll. In addition, chlorophyllide a can be transformed into chlorophyllide b, chlorophyllide d, or chlorophyllide f. Chlorophyllide c can be synthesized from protochlorophyllide a or divinyl protochlorophyllide a. Chlorophyllides have been extensively used in food, medicine, and pharmaceutical applications. Furthermore, chlorophyllides exhibit many biological activities, such as anti-growth, antimicrobial, antiviral, antipathogenic, and antiproliferative activity. The photosensitivity of chlorophyllides that is applied in mercury electrodes and sensors were discussed. This article is the first detailed review dedicated specifically to chlorophyllides. Thus, this review aims to describe the definition of chlorophyllides, biosynthetic routes of chlorophyllides, purification of chlorophyllides, and applications of chlorophyllides.
Protochlorophyllide
Tetrapyrrole
Photosensitivity
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Protochlorophyllide
Tetrapyrrole
Protoporphyrin IX
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The key step in chlorophyll biosynthesis is photoreduction of its immediate precursor, protochlorophyllide. This reaction is catalyzed by a photoenzyme, protochlorophyllide oxidoreductase (POR) and consists in the attachment of two hydrogen atoms in positions C17 and C18 of the tetrapyrrole molecule of protochlorophyllide; the double bond is replaced with the single bond. Two hydrogen donors involved in protochloro-phyllide photoreduction are NADPH [1,2] and a conserved tyrosine residue Tyr193 of the photoenzyme POR [3]. The structure of active pigment-enzyme complex (Pchlide-POR-NADPH) ensures a favorable steric conditions for the transfer of hydride ion and proton. This review does not examine the ternary complex structure, but concentrates upon the mechanisms of primary photophysical and photochemical reactions during formation of chlorophyllide from protochlorophyllide in living objects (etiolated leaves and leaf homogenates) and model systems.
Protochlorophyllide
Tetrapyrrole
Ternary complex
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Protochlorophyllide
Tetrapyrrole
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Pyrroles and pyridiniums (structurally related to a tetrapyrrole quadrant), and dipyridyls (structurally related to a tetrapyrrole half) were evaluated for their photodynamic herbicidal effects in cucumber (Cucumis sativus L.). The ability of these modulators to induce the accumulation of large amounts of porphyrins viz., protoporphyrin IX (Proto), magnesium-Proto and magnesium-Proto monomethylester (MPE), and protochlorophyllide (Pchlide) in the presence or absence of exogenous δ-aminolevulinic acid (ALA) was also investigated. Substituted pyrroles exhibited moderate photodynamic herbicidal effects and caused the accumulation of Pchlide only. Pyridinium analogues induced significant amounts of MPE or Pchlide accumulation and caused photodynamic injury. Dipyridyls caused greater photodynamic herbicidal injury than either pyrroles or pyridiniums, and induced the accumulation of Proto as well.
Tetrapyrrole
Protochlorophyllide
Protoporphyrinogen oxidase
Protoporphyrin IX
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Protochlorophyllide
Tetrapyrrole
Hemeprotein
Protoporphyrin IX
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