Fusicocca-3(16),10(14)-diene, and β- and δ-Araneosenes, New Fusicoccin Biosynthesis-related Diterpene Hydrocarbons from<i>Phomopsis amygdali</i>

Sassa, Takeshi; Kenmoku, Hiromichi; Nakayama, Kayoko; Kato, Nobuo

doi:10.1271/bbb.68.1608

Cited by 13 publications

(14 citation statements)

References 8 publications

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“…3 A and C) were identical to those of authentic fusicocca-2,10 (14)-diene ( Fig. 3 B, peak 2, and D) (30). Nine by-products related to fusicoccadiene were detected, of which eight were minor peaks.…”

Section: Pafs Encodes Fusicocca-210 (14)-diene Synthase Also Possesssupporting

confidence: 59%

Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi

Toyomasu

Tsukahara

Kaneko

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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186

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Fusicoccins are a class of diterpene glucosides produced by the plant-pathogenic fungus Phomopsis amygdali. As modulators of 14-3-3 proteins, fusicoccins function as potent activators of plasma membrane H ؉ -ATPase in plants and also exhibit unique biological activity in animal cells. Despite their well studied biological activities, no genes encoding fusicoccin biosynthetic enzymes have been identified. Cyclic diterpenes are commonly synthesized via cyclization of a C20 precursor, geranylgeranyl diphosphate (GGDP), which is produced through condensation of the universal C5 isoprene units dimethylallyl diphosphate and isopentenyl diphosphate by prenyltransferases. We found that (؉)-fusicocca-2,10 (14)-diene, a tricyclic hydrocarbon precursor for fusicoccins, is biosynthesized from the C5 isoprene units by an unusual multifunctional enzyme, P. amygdali fusicoccadiene synthase (PaFS), which shows both prenyltransferase and terpene cyclase activities. The functional analysis of truncated mutants and site-directed mutagenesis demonstrated that PaFS consists of two domains: a terpene cyclase domain at the N terminus and a prenyltransferase domain at the C terminus. These findings suggest that fusicoccadiene can be produced efficiently in the fungus by using the C5 precursors, irrespective of GGDP availability. In fact, heterologous expression of PaFS alone resulted in the accumulation of fusicocca-2,10 (14)-diene in Escherichia coli cells, whereas no product was detected in E. coli cells expressing Gibberella fujikuroi ent-kaurene synthase, another fungal diterpene cyclase that also uses GGDP as a substrate but does not contain a prenyltransferase domain. Genome walking suggested that fusicoccin biosynthetic enzymes are encoded as a gene cluster near the PaFS gene.biosynthesis ͉ cyclase ͉ prenyltransferase F usicoccins (FC) A (1, 2) and J (3, 4) ( Fig. 1) are the major metabolites produced by the plant-pathogenic fungus Phomopsis (Fusicoccum) amygdali (Del.) (5). Fusicoccin A and the structurally related cotylenins (CN) (6-8), e.g., cotylenin A (Fig.

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Section: Pafs Encodes Fusicocca-210 (14)-diene Synthase Also Possesssupporting

confidence: 59%

Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi

Toyomasu

Tsukahara

Kaneko

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

186

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“…These results suggest that P. amygdali N2 did not produce any labdane-related compounds, 14) probably owing to the suppression of PaDC1 expression and loss of function of the C-terminal type A cyclization domain of PaDC2.…”

Section: Functions Of Padc1 and Padc2mentioning

confidence: 86%

“…In the mycelia of P. amygdali N2, fusicoccadiene-related hydrocarbons make up most of the hydrocarbon fraction. 14) However, in the hydrocarbon fraction of the extract from the mycelia of P. amygdali F6, several labdane-related hydrocarbons derived from (+)-CDP were detected, in addition to the foregoing hydrocarbons. 14) We therefore performed RT-PCR, using as The filled inverted triangle indicates the starting point for genome walking.…”

Section: Isolation Of Orf Cdnas Of Padc1 and Padc2mentioning

confidence: 94%

“…14) However, in the hydrocarbon fraction of the extract from the mycelia of P. amygdali F6, several labdane-related hydrocarbons derived from (+)-CDP were detected, in addition to the foregoing hydrocarbons. 14) We therefore performed RT-PCR, using as The filled inverted triangle indicates the starting point for genome walking. These nucleotide sequences of A and B have been deposited in the databases with accession numbers AB254158 and AB254160, respectively.…”

Section: Isolation Of Orf Cdnas Of Padc1 and Padc2mentioning

confidence: 94%

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Identification of Diterpene Biosynthetic Gene Clusters and Functional Analysis of Labdane-Related Diterpene Cyclases inPhomopsis amygdali

Toyomasu¹,

Niida²,

Kenmoku³

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…The conversion of fusicocca-2,10(14)-diene from GGDP has been shown to be initiated by ionization of the allylic diphosphate group. 48) We isolated a homolog of PaDC3:GGS, by RT-PCR with degenerate primers, which we named PaFS. It has been demonstrated that recombinant PaFS converts GGDP into fusicocca-2,10(14)-diene.…”

Section: Labdane-related Diterpene Cyclase Gene Family In Ricementioning

confidence: 99%

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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Fusicocca-3(16),10(14)-diene, and β- and δ-Araneosenes, New Fusicoccin Biosynthesis-related Diterpene Hydrocarbons fromPhomopsis amygdali

Cited by 13 publications

References 8 publications

Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi

Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi

Identification of Diterpene Biosynthetic Gene Clusters and Functional Analysis of Labdane-Related Diterpene Cyclases inPhomopsis amygdali

Recent Advances Regarding Diterpene Cyclase Genes in Higher Plants and Fungi

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