scholarly journals The cyanobacteriumGloeobacter violaceusPCC 7421 uses bacterial-type phytoene desaturase in carotenoid biosynthesis

FEBS Letters ◽  
2005 ◽  
Vol 579 (10) ◽  
pp. 2125-2129 ◽  
Author(s):  
Tohru Tsuchiya ◽  
Shinichi Takaichi ◽  
Norihiko Misawa ◽  
Takashi Maoka ◽  
Hideaki Miyashita ◽  
...  
Keyword(s):  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Bacterial Type

Photoregulation of Carotenoid Biosynthesis in Mutants of Neurospora crassa: Activities of Enzymes Involved in the Synthesis and Conversion of Phytoene

1993 ◽  
Vol 48 (7-8) ◽  
pp. 570-574 ◽  
Author(s):  
Gerhard Sandmann
Keyword(s):  
Neurospora Crassa ◽  
Enzyme Level ◽  
Light Regulation ◽  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Farnesyl Pyrophosphate ◽  
Farnesyl Pyrophosphate Synthase ◽  
Geranylgeranyl Pyrophosphate Synthase ◽  
Lycopene Cyclase ◽  
Carotenoid Mutants

Synthesis of carotenoids is photoregulated in many fungi including Neurospora crassa. In order to investigate the regulatory mechanism at the enzyme level, several carotenoid mutants of Neurospora were used to determine the activities of enzymes involved in the carotenoid bio synthetic pathway after growth under illumination or in darkness. Light stimulation of carotenoid formation was due to enhanced activities of three subsequent enzymes, geranylgeranyl pyrophosphate synthase, phytoene synthase, and phytoene desaturase indicating a coordinated regulation at the enzyme level. Farnesyl pyrophosphate synthase and lycopene cyclase were not involved in light regulation. Immunological studies showed that in the case of phytoene desaturase higher activity in the light originated from an increased amount of this enzyme in light-grown cultures.

The discovery and structural requirements of inhibitors of p-hydroxyphenylpyruvate dioxygenase

Weed Science ◽  
1997 ◽  
Vol 45 (5) ◽  
pp. 601-609 ◽  
Author(s):  
David L. Lee ◽  
Michael P. Prisbylla ◽  
Thomas H. Cromartie ◽  
Derek P. Dagarin ◽  
Stott W. Howard ◽  
...  
Keyword(s):  
Mechanism Of Action ◽  
Biosynthetic Pathway ◽  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Rat Urine ◽  
Meristematic Tissue ◽  
Chemically Induced ◽  
Mammalian Enzyme ◽  
Unique Mechanism

The benzoylcyclohexane-1,3-diones, the triketones, are potent bleaching herbicides whose structure-activity relationships and physical properties are substantially different from classical bleaching herbicides, which affect phytoene desaturase. The first clue to their unique mechanism of action was the discovery that rats treated with a triketone were found to be tyrosinemic. Additionally, examination of the rat urine revealed the accumulation of p-hydroxyphenylpyruvate (HPP) and p-hydroxyphenyllactate. These results suggested that this chemically induced tyrosinemia was the result of the inhibition of p-hydroxyphenylpyruvate dioxygenase (HPPD, EC 1.13.11.27), and this suggestion was confirmed when a triketone was shown to be a potent inhibitor of rat liver HPPD. In plants, HPPD is a component of the biosynthetic pathway to plastoquinone (PQ), which in turn is a key cofactor of phytoene desaturase. The expectation that triketone-treated plants should accumulate tyrosine while having reduced PQ levels was dramatically demonstrated in the meristematic tissue of ivyleaf morningglory. Plant HPPD, like the mammalian enzyme, was inhibited in vitro by triketones. These biochemical effects provide evidence that the triketone herbicidal mechanism of action is HPPD inhibition leading to a deficiency of PQ, a key cofactor for carotenoid biosynthesis. Other chemical classes of bleaching herbicides were also examined for their ability to elevate tyrosine and deplete PQ as a definitive means of establishing their mode of action and for delineating the structural and physical chemical requirements for an HPPD herbicide. Evidence is provided to support the claim that a 2-benzoylethen-1-ol substructure is the minimum substructure required for a potent HPPD inhibitor.

Molecular Characterization of Carotenoid Biosynthesis in Plants: The Phytoene Desaturase Gene in Tomato

1992 ◽  
pp. 11-18 ◽  
Author(s):  
Iris Pecker ◽  
Daniel Chamovitz ◽  
Varda Mann ◽  
Gerhard Sandmann ◽  
Peter Böger ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Desaturase Gene

scholarly journals Silencing of the phytoene desaturase (PDS) gene affects the expression of fruit-ripening genes in tomatoes

Plant Methods ◽  
2019 ◽  
Vol 15 (1) ◽  
Author(s):  
Aung Htay Naing ◽  
Swum Yi Kyu ◽  
Phyo Phyo Win Pe ◽  
Kyeung Il Park ◽  
Je Min Lee ◽  
...  
Keyword(s):  
Gene Silencing ◽  
Fruit Ripening ◽  
Tomato Fruit ◽  
Carotenoid Biosynthesis ◽  
Past Research ◽  
Ethylene Biosynthesis ◽  
Phytoene Desaturase ◽  
Virus Induced Gene Silencing ◽  
Pale Yellow ◽  
Ripening Genes

Abstract Background Past research has shown that virus-induced phytoene desaturase (PDS) gene silencing via agroinjection in the attached and detached fruit of tomato plants results in a pale-yellow fruit phenotype. Although the PDS gene is often used as a marker for gene silencing in tomatoes, little is known about the role of PDS in fruit ripening. In this study, we investigated whether the pepper PDS gene silenced endogenous PDS genes in the fruit of two tomato cultivars, Dotaerang Plus and Legend Summer. Results We found that the pepper PDS gene successfully silenced endogenous PDS in tomato fruit at a silencing frequency of 100% for both cultivars. A pale-yellow silenced area was observed over virtually the entire surface of individual fruit due to the transcriptional reduction in phytoene desaturase (PDS), zeta-carotene (ZDS), prolycopene isomerase (CrtlSO), and beta-carotene hydroxylase (CrtR-b2), which are the carotenoid biosynthesis genes responsible for the red coloration in tomatoes. PDS silencing also affected the expression levels of the fruit-ripening genes Tomato AGAMOUS-LIKE1 (TAGL1), RIPENING INHIBITOR (RIN), pectin esterase gene (PE), lipoxygenase (LOX), FRUITFULL1/FRUITFUL2 (FUL1/FUL2), and the ethylene biosynthesis and response genes 1-aminocyclopropane-1-carboxylate oxidase 1 and 3 (ACO1 and ACO3) and ethylene-responsive genes (E4 and E8). Conclusion These results suggest that PDS is a positive regulator of ripening in tomato fruit, which must be considered when using it as a marker for virus-induced gene silencing (VIGS) experiments in order to avoid fruit-ripening side effects.

Transformation of Tobacco with a Mutated Cyanobacterial Phytoene Desaturase Gene Confers Resistance to Bleaching Herbicides

2002 ◽  
Vol 57 (7-8) ◽  
pp. 671-679 ◽  
Author(s):  
Tobias Wagner ◽  
Ute Windhövel ◽  
Susanne Römer
Keyword(s):  
Genetic Manipulation ◽  
Enzymatic Reaction ◽  
Photosynthetic Apparatus ◽  
D1 Protein ◽  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Desaturase Gene ◽  
Synechococcus Pcc 7942 ◽  
Pcc 7942 ◽  
Transformed Tobacco

Carotenoids are constituents of the photosynthetic apparatus and essential for plant survival because of their involvement in protection of chlorophylls against photooxidation. Certain classes of herbicides are interfering with carotenoid biosynthesis leading to pigment destruction and a bleached plant phenotype. One important target site for bleaching herbicides is the enzyme phytoene desaturase catalysing the desaturation of phytoene in ζ-carotene. This enzymatic reaction can be inhibited by norflurazon or fluridone. We have transformed tobacco with a mutated cyanobacterial phytoene desaturase gene (pds) derived from the Synechococcus PCC 7942 mutant NFZ4. Characterization of the resulting transformants revealed an up to 58 fold higher norflurazon resistance in comparison to wild type controls. The tolerance for fluridone was also increased 3 fold in the transgenics. Furthermore, the transformed tobacco maintained a higher level of D1 protein of photosystem II indicating a lower susceptibility to photooxidative damage in the presence of norflurazon. In contrast, the genetic manipulation did not confer herbicide resistance against ζ-carotene desaturase inhibitors.

scholarly journals Transformation of the Green Alga Haematococcus pluvialis with a Phytoene Desaturase for Accelerated Astaxanthin Biosynthesis

2006 ◽  
Vol 72 (12) ◽  
pp. 7477-7484 ◽  
Author(s):  
Jens Steinbrenner ◽  
Gerhard Sandmann
Keyword(s):  
Green Alga ◽  
Haematococcus Pluvialis ◽  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Site Directed Mutagenesis ◽  
Carotenoid Content ◽  
Desaturase Gene ◽  
Vitro Assay ◽  
Gene And Protein Expression

ABSTRACT Astaxanthin is a high-value carotenoid which is used as a pigmentation source in fish aquaculture. Additionally, a beneficial role of astaxanthin as a food supplement for humans has been suggested. The unicellular alga Haematococcus pluvialis is a suitable biological source for astaxanthin production. In the context of the strong biotechnological relevance of H. pluvialis, we developed a genetic transformation protocol for metabolic engineering of this green alga. First, the gene coding for the carotenoid biosynthesis enzyme phytoene desaturase was isolated from H. pluvialis and modified by site-directed mutagenesis, changing the leucine codon at position 504 to an arginine codon. In an in vitro assay, the modified phytoene desaturase was still active in conversion of phytoene to ζ-carotene and exhibited 43-fold-higher resistance to the bleaching herbicide norflurazon. Upon biolistic transformation using the modified phytoene desaturase gene as a reporter and selection with norflurazon, integration into the nuclear genome of H. pluvialis and phytoene desaturase gene and protein expression were demonstrated by Southern, Northern, and Western blotting, respectively, in 11 transformants. Some of the transformants had a higher carotenoid content in the green state, which correlated with increased nonphotochemical quenching. This measurement of chlorophyll fluorescence can be used as a screening procedure for stable transformants. Stress induction of astaxanthin biosynthesis by high light showed that there was accelerated accumulation of astaxanthin in one of the transformants compared to the accumulation in the wild type. Our results strongly indicate that the modified phytoene desaturase gene is a useful tool for genetic engineering of carotenoid biosynthesis in H. pluvialis.

Inhibition of Phytoene Desaturase – the Mode of Action of Certain Bleaching Herbicides

1984 ◽  
Vol 39 (5) ◽  
pp. 443-449 ◽  
Author(s):  
Gerhard Sandmann ◽  
Ian E. Clarke ◽  
Peter M. Bramley ◽  
Peter Böger
Keyword(s):  
Comparative Study ◽  
Mode Of Action ◽  
Inhibitory Action ◽  
Carotenoid Biosynthesis ◽  
Phytoene Desaturase ◽  
Target Site ◽  
Primary Target ◽  
Pigment Degradation ◽  
A Cell ◽  
Lipophilic Groups

Assay systems have been developed in order to differentiate between the modes of action of certain bleaching herbicides. These include inhibition of chlorophyll or carotenoid biosynthesis, and initiation of pigment degradation. Herbicidal compounds with phytoene desaturase as their primary target site were investigated in a cell-free carotenogenic system from Aphanocapsa. In a comparative study, the structural prerequisites for inhibition of phytoene desaturase were established for both benzophenone analogs and various m-phenoxybenzamides. This inhibitory action of the latter compounds is enhanced by lipophilic groups with certain steric properties.

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