The structure of fusicoccin A

Ballio, A.; Brufani, M.; Casinovi, C. G.; Cerrini, S.; Fedeli, W.; Pellicciari, R.; Santurbano, B.; Vaciago, A.

doi:10.1007/bf02153818

Cited by 148 publications

(61 citation statements)

References 5 publications

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“…3) are representative metabolites produced by the phytopathogenic fungus Phomopsis (Fusicoccum) amygdali (Del.). 16,39) Fusicoccin A not only has potent higher plant plasma membrane H þ -ATPase-activating activity, 17) but also exerts effects on amphibian embryogenesis. 40) The aglycon of fusicoccins is a tricyclic diterpene derived from GGDP.…”

Section: Labdane-related Diterpene Cyclase Gene Family In Ricementioning

confidence: 99%

“…1) [10][11][12] have been isolated from plants. Similarly, fungal GAs, 13) aphidicolin (a specific inhibitor of DNA polymerase ), 14,15) and fusicoccin A (a diterpene glucoside that acts as a plant plasma membrane H þ -ATPase activator) 16,17) have been isolated from fungi. The cyclic carbon skeletons of these diterpenoids are elaborated from a common precursor, GGDP, and the formation of the cyclic hydrocarbons is catalyzed by specific diterpene cyclases.…”

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confidence: 99%

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Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

Toyomasu

2008

Bioscience, Biotechnology, and Biochemistry

100

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Cyclic diterpenoids are commonly biosynthesized from geranylgeranyl diphosphate (GGDP) through the formation of carbon skeletons by specific cyclases and subsequent chemical modifications, such as oxidation, reduction, methylation, and glucosidation. A variety of diterpenoids are produced in higher plants and fungi. Rice produces four classes of diterpene phytoalexins, phytocassanes A to E, oryzalexins A to F, oryzalexin S, and momilactones A and B. The six diterpene cyclase genes involved in the biosynthesis of these phytoalexins were identified and characterized. Fusicoccin A was produced by the phytopathogenic Phomopsis amygdali and served as a plant H þ -ATPase activator. A PaFS, encoding a fungal diterpene synthase responsible for fusicoccin biosynthesis, was isolated. The PaFS is an unusual chimeric diterpene synthase that possesses not only terpene cyclase activity (the formation of fusicoccadiene, a biosynthetic precursor of fusicoccin A), but also prenyltransferase activity (the formation of GGDP). Thus, we identified a unique multifunctional diterpene synthase family in fungi.

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Section: Labdane-related Diterpene Cyclase Gene Family In Ricementioning

confidence: 99%

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confidence: 99%

Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

Toyomasu

2008

Bioscience, Biotechnology, and Biochemistry

100

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“…FC3, a phytotoxin isolated from the fungus Fusicoccum amygdali (2), rapidly stimulates net H+ efflux and K+ uptake in practically all higher plant tissues so far examined (17). FC has also been reported to stimulate plant cell enlargement (4,19,24), to cause rapid stomatal opening (25), and to promote seed germination (13).…”

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Partial Characterization of Fusicoccin Binding to Receptor Sites on Oat Root Membranes

Stout¹,

Cleland²

1980

Plant Physiol.

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The possibility that fusicoccin (FC) binds to plasma membrane-associated ATPases of oat (cv. Victory) roots has been examined. Specific FC-binding in viro is localized primarily on plasma membrane-enriched fractions. This FC-binding is greatly reduced by pretreatment of the membrane vesicles at temperatures above 45 C or with trypsin, and the same treatments cause the release of already bound FC. These results support the idea that the FC receptor is a protein located on the plasma membrane.Both active ATPases and FC-bndlng proteins were solubilized using 1% Triton X-100. When this material was fractionated using gel chromatography, the ATPase activity could be separated from the FC-bnding proteins. The identity of the FC-binding proteins is discussed with regard to the extensive evidence which supports the involvement of plasma membrane-ATPase H+/K+ pumps in FC-stimulated aciification and K+ uptake.FC3, a phytotoxin isolated from the fungus Fusicoccum amygdali (2), rapidly stimulates net H+ efflux and K+ uptake in practically all higher plant tissues so far examined (17). FC has also been reported to stimulate plant cell enlargement (4,19,24), to cause rapid stomatal opening (25), and to promote seed germination (13). It has been suggested that the effects ofFC on these important physiological processes may be a consequence of an FC-activated increase in H /K+ exchange across the plasma membrane (16). Inasmuch as, in some instances, FC mimics the action of natural plant hormones (17), an understanding ofthe mechanism ofaction of FC may aid not only in the study of membrane transport in plants but also in studies on the mechanism of action of plant hormones.The rapidity of the effects of FC on H+ and K+ transport (5, 21) and on hyperpolarization of the membrane potential (7, Seeds ofA vena sativa L cv. Victory were germinated and grown hydroponically using the culture techniques of Hodges and Leonard (9). The oat seeds were grown in the dark for 4 to 5 days at about 25 C over a vigorously aerated solution of I mm CaSO4. Whole roots (5-10 cm long) were excised and washed two to three times with cold distilled H20 prior to homogenization.Alternatively, seeds were sown on moist Vermiculite and grown in the dark at 28 C for 4 to 5 days. Intact seedlings were gently removed, and the roots were washed in distilled H20 to remove the Vermiculite. The excised roots were washed three times with cold distilled H20 before homogenization. Bacterial contamination of the oat roots grown in this manner was determined, and it was found that, after three washes in distilled H20, bacterial levels were reduced to about 104 bacteria/g fresh weight of tissue (Table I). No detectable differences in amount or activity of ATPases of the PM-enriched fractions were found between roots grown hydroponically and in Vermiculite.Membrane Fraction Preparation. The procedures of Hodges and Leonard (9) were used to isolate membrane fractions, and all operations were carried out at 0 to 5 C. The roots were first chopped up with a razor ...

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“…FC was prepared according to Ballio et al [23]. Tritiated dihydro-FC (rH]FC) was obtained as described by Ballio et al [24]; its specific activity was 20.5 Cilmmol.…”

Section: Chemicals and Enzymesmentioning

confidence: 99%

Phospholipase A₂ affects the activity of fusicoccin receptors

et al. 1993

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Biochemical properties of fusicoccin receptors are strongly influenced by the phospholipid environment. In this report we have studied the effect of different exogenous phospholipases on fusicoccin binding ability of both plasma membrane and solubilised receptors. Among the phospholipases tested only phospholipase A, showed an inhibitory effect on fusicoccin binding. In particular, the influence of this enzyme on the time course and reversibility of the fusicoccin binding reaction was studied. The inhibitory effect of phospholipase A, was the consequence of fatty acid release. The usual fatty acids of plasma membrane phospholipids were active in inhibiting the interaction of fusicoccin with its receptors. It is concluded that a phospholipid associated to the fusicoccin receptor might play a significant role in the modulation of binding.Fusicoccin; Membrane receptor; Zeu mays L.

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The structure of fusicoccin A

Cited by 148 publications

References 5 publications

Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

Partial Characterization of Fusicoccin Binding to Receptor Sites on Oat Root Membranes

Phospholipase A₂ affects the activity of fusicoccin receptors

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The structure of fusicoccin A

Cited by 148 publications

References 5 publications

Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

Partial Characterization of Fusicoccin Binding to Receptor Sites on Oat Root Membranes

Phospholipase A2 affects the activity of fusicoccin receptors

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Phospholipase A₂ affects the activity of fusicoccin receptors