The geranylgeranyl diphosphate synthase gene of Gibberella fujikuroi: isolation and expression

Mende, Katrin; Homann, Veronika; Tudzynski, Bettina

doi:10.1007/s004380050477

Cited by 67 publications

(46 citation statements)

References 49 publications

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“…In F. fujikuroi, two GGDP synthase-encoding genes, ggs1 (36) and ggs2 (58), have been characterized. One of them, ggs2, is located in the GA biosynthetic gene cluster and is specifically involved in GA production, whereas no pathway-specific ggs gene has been found so far in the F. fujikuroi carotenoid gene cluster (J. Avalos, personal communication).…”

Section: Discussionmentioning

confidence: 99%

“…1). In F. fujikuroi, two GGDP synthase-encoding genes, ggs1 (36) and ggs2 (58), the latter located in the GA gene cluster, have been found. Interestingly, GGDP for GA biosynthesis is specifically produced by GGS2, as disruption of the corresponding gene, ggs2, resulted in the total loss of GA production, while ggs1, which is responsible for general terpenoid biosynthesis, was unable to complement the block at GGS2 (B. Tudzynski, unpublished data).…”

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Restoration of Gibberellin Production in Fusarium proliferatum by Functional Complementation of Enzymatic Blocks

Malonek

Rojas

Hedden

et al. 2005

Appl Environ Microbiol

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Nine biological species, or mating populations (MPs), denoted by letters A to I, and at least 29 anamorphic Fusarium species have been identified within the Gibberella fujikuroi species complex. Members of this species complex are the only species of the genus Fusarium that contain the gibberellin (GA) biosynthetic gene cluster or at least parts of it. However, the ability of fusaria to produce GAs is so far restricted to Fusarium fujikuroi, although at least six other MPs contain all the genes of the GA biosynthetic gene cluster. Members of Fusarium proliferatum, the closest related species, have lost the ability to produce GAs as a result of the accumulation of several mutations in the coding and 5 noncoding regions of genes P450-4 and P450-1, both encoding cytochrome P450 monooxygenases, resulting in metabolic blocks at the early stages of GA biosynthesis. In this study, we have determined additional enzymatic blocks at the first specific steps in the GA biosynthesis pathway of F. proliferatum: the synthesis of geranylgeranyl diphosphate and the synthesis of ent-kaurene. Complementation of these enzymatic blocks by transferring the corresponding genes from GA-producing F. fujikuroi to F. proliferatum resulted in the restoration of GA production. We discuss the reasons for Fusarium species outside the G. fujikuroi species complex having no GA biosynthetic genes, whereas species distantly related to Fusarium, e.g., Sphaceloma spp. and Phaeosphaeria spp., produce GAs.

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Restoration of Gibberellin Production in Fusarium proliferatum by Functional Complementation of Enzymatic Blocks

Malonek

Rojas

Hedden

et al. 2005

Appl Environ Microbiol

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“…Like the paxilline biosynthesis cluster in P. paxilli, the gibberellin and aphidicolin gene clusters contain a GGPP synthase gene, named ggs-2 and Pbggs, respectively. P. paxilli and F. fujikuroi also carry a second GGPP synthase gene, suggesting that the presence of two copies of GGPP synthase may be a molecular signature for diterpene biosynthesis (28,53). Given that many genes for secondary metabolite biosynthesis in fungi are organized in clusters (23), the molecular cloning of GGPP synthases combined with chromosome walking could provide a rapid strategy for cloning new indole-diterpene gene clusters.…”

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Indole-Diterpene Gene Cluster fromAspergillus flavus

Zhang

Monahan

Tkacz

et al. 2004

Appl Environ Microbiol

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Aflatrem is a potent tremorgenic mycotoxin produced by the soil fungus Aspergillus flavus and is a member of a large structurally diverse group of secondary metabolites known as indole-diterpenes. By using degenerate primers for conserved domains of fungal geranylgeranyl diphosphate synthases, we cloned two genes, atmG and ggsA (an apparent pseudogene), from A. flavus. Adjacent to atmG are two other genes, atmC and atmM. These three genes have 64 to 70% amino acid sequence similarity and conserved synteny with a cluster of orthologous genes, paxG, paxC, and paxM, from Penicillium paxilli which are required for indole-diterpene biosynthesis. atmG, atmC, and atmM are coordinately expressed, with transcript levels dramatically increasing at the onset of aflatrem biosynthesis. A genomic copy of atmM can complement a paxM deletion mutant of P. paxilli, demonstrating that atmM is a functional homolog of paxM. Thus, atmG, atmC, and atmM are necessary, but not sufficient, for aflatrem biosynthesis by A. flavus. This provides the first genetic evidence for the biosynthetic pathway of aflatrem in A. flavus.Aflatrem is a potent tremorgenic mycotoxin produced by the soil fungus Aspergillus flavus (17,18). This compound is a member of a large, structurally diverse group of secondary metabolites known as indole-diterpenes that includes paspaline, paxilline, shearinines, paspalitrems, terpendoles, penitrems, lolitrems, janthitrems, and sulpinines (34). These metabolites all have a common structural core comprised of a cyclic diterpene skeleton derived from geranylgeranyl diphosphate (GGPP) and an indole moiety derived from either tryptophan or a tryptophan precursor. Different patterns of prenylation, hydroxylation, epoxidation, acetylation, and ring stereochemistry around the basic indole-diterpene ring structure define this structural diversity (34). The mechanism by which aflatrem and related indole-diterpenes cause tremorgenicity in mammals is not well defined, but biochemical and clinical studies indicate that these effects are due in part to effects on receptors and to interference with neurotransmitter release in the central and peripheral nervous systems (40).Very little is known about the pathways of indole-diterpene biosynthesis other than the origins of the indole and diterpene components (7, 10). Biosynthetic schemes based on the chemical identification of likely intermediates have been proposed, but until recently none of these steps had been validated by biochemical or genetic studies (25,30).Recently, a cluster of genes for paxilline biosynthesis was cloned from Penicillium paxilli (53). Key genes in this cluster include a GGPP synthase gene (paxG), a FAD-dependent monooxygenase gene (paxM), a prenyl transferase gene (paxC), and two cytochrome P450 monooxygenase genes, paxP and paxQ. The deletion of paxG, paxM, or paxC results in mutants that are defective in paxilline biosynthesis (53; B. Scott, L. McMillan, J. Astin, C. Young, A. Bryant, and E.Parker, unpublished results). PaxM and PaxC may catalyze the additi...

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“…Thus, GGPP synthase is a crucial branch point enzyme that is responsible for the various aspects of plant growth and development. The mechanism for the enzymatic reaction with condensation of isopentenyl diphosphate (IPP) and other substrates such as farnesyl diphosphate (FPP) to produce C 20 GGPP is conserved among organisms from bacteria (Mende et al, 1997) to humans (Kainou et al, 1999).…”

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Five Geranylgeranyl Diphosphate Synthases Expressed in Different Organs Are Localized into Three Subcellular Compartments in Arabidopsis

Okada

Saito²,

Nakagawa³

et al. 2000

Plant Physiology

238

204

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Geranylgeranyl diphosphate (GGPP) is the precursor for the biosynthesis of gibberellins, carotenoids, chlorophylls, isoprenoid quinones, and geranylgeranylated proteins in plants. There is a small gene family for GGPP synthases encoding five isozymes and one related protein in Arabidopsis, and all homologs have a putative localization signal to translocate into specific subcellular compartments. Using a synthetic green fluorescent protein (sGFP), we studied the subcellular localization of these GGPP synthases. When these fusion proteins were expressed by the cauliflower mosaic virus 35S promoter in Arabidopsis, GGPS1-sGFP and GGPS3-sGFP proteins were translocated into the chloroplast, GGPS2-sGFP and GGPS4-sGFP proteins were localized in the endoplasmic reticulum, and the GGPS6-sGFP protein was localized in the mitochondria. Both GGPS1 and GGPS3 proteins synthesized in vitro were taken up into isolated intact pea chloroplasts and processed to the mature form. RNA-blot and promoter-␤-glucuronidase (GUS) analysis showed that these GGPP synthases genes are organ-specifically expressed in Arabidopsis. GGR and GGPS1 were ubiquitously expressed, while GGPS2, GGPS3, and GGPS4 were expressed specifically in the flower, root, and flower, respectively. These results suggest that each GGPP synthase gene is expressed in different tissues during plant development and GGPP is synthesized by the organelles themselves rather than being transported into the organelles. Therefore, we predict there will be specific pathways of GGPP production in each organelle.

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The geranylgeranyl diphosphate synthase gene of Gibberella fujikuroi: isolation and expression

Cited by 67 publications

References 49 publications

Restoration of Gibberellin Production in Fusarium proliferatum by Functional Complementation of Enzymatic Blocks

Restoration of Gibberellin Production in Fusarium proliferatum by Functional Complementation of Enzymatic Blocks

Indole-Diterpene Gene Cluster fromAspergillus flavus

Five Geranylgeranyl Diphosphate Synthases Expressed in Different Organs Are Localized into Three Subcellular Compartments in Arabidopsis

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