4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon : purification of a plant membrane-bound prenyltransferase

Mühlenweg, Agnes; Melzer, Martin; Li, Shu-Ming; Heide, Lutz

doi:10.1007/s004250050337

Cited by 45 publications

(34 citation statements)

References 34 publications

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“…Other groups extended these results using additional plant cell cultures, e.g. parsley (Petroselinum crispum; Dittrich et al, 1992), Taxus cuspidata (Mirjalili and Linden, 1996), rice (Norjiri et al, 1996) or Lithospermum erythrorhizon (Mühlenweg et al, 1998). Remarkably, the treatment with JA did not result for all species in the production of phytoalexins, inducible low molecular weight compounds with antimicrobial properties correlating with plant defense.…”

Section: Introductionmentioning

confidence: 93%

The Role of Octadecanoids and Functional Mimics in Soybean Defense Responses

Fliegmann

Schüler

Boland

et al. 2003

Biological Chemistry

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Oxylipins of the jasmonate pathway and synthetic functional analogs have been analyzed for their elicitor-like activities in an assay based on the induced accumulation of glyceollins, the phytoalexins of soybean (Glycine max L.), in cell suspension cultures of this plant. Jasmonic acid (JA) and its methyl ester showed weak phytoalexin-inducing activity when compared to an early jasmonate biosynthetic precursor, 12-oxo-phytodienoic acid (OPDA), as well as to the bacterial phytotoxin coronatine and certain 6-substituted indanoyl-L-isoleucine methyl esters, which all were highly active. Interestingly, different octadecanoids and indanoyl conjugates induced the accumulation of transcripts of various defense-related genes to different degrees, indicating distinct induction competencies. Therefore, these signaling compounds and mimics were further analyzed for their effects on signal transduction elements, such as the transient enhancement of the cytosolic Ca 2 + concentration and MAP kinase activation, which are known to be initiated by a soybean pathogen-derived ␤-glucan elicitor. In contrast to the ␤-glucan elicitor, none of the other compounds tested triggered these early signaling elements. Moreover, endogenous levels of OPDA and JA in soybean cells were shown to be unaffected after treatment with ␤-glucans. Thus, OPDA and JA, which are functionally mimicked by coronatine and a variety of 6-substituted derivatives of indanoyl-L-isoleucine methyl ester, represent highly efficient signaling compounds of a lipid-based pathway not deployed in the ␤-glucan elicitor-initiated signal transduction.

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Section: Introductionmentioning

confidence: 93%

The Role of Octadecanoids and Functional Mimics in Soybean Defense Responses

Fliegmann

Schüler

Boland

et al. 2003

Biological Chemistry

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“…The corresponding region in E. coli UbiA and COQ2, the UbiA orthologue of Saccharomyces cerevisiae, was predicted to be the prenyl diphosphate-binding site, suggesting that archaeal DGGGPSs catalyze prenyl transfer reactions via the same mechanism as the other UbiA-related prenyltransferases. Moreover, all the enzymes classified in this family are considered to be, and some have been shown (22,23), to be membrane-intrinsic, unlike other prenyltransferases such as GGPS and GGGPS. In fact, the hydrophobicity plot of S. solfataricus DGGGPS was very similar with that of E. coli UbiA, and they clearly show that the enzymes contain multiple transmembrane regions (data not shown).…”

Section: Gggp By Negative-mode Fab-ms: An Ion Peak With An M/z Value mentioning

confidence: 99%

(S)-2,3-Di-O-geranylgeranylglyceryl Phosphate Synthase from the Thermoacidophilic Archaeon Sulfolobus solfataricus

Hemmi

Shibuya

Takahashi

et al. 2004

Journal of Biological Chemistry

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The core structure of membrane lipids of archaea have some unique properties that permit archaea to be distinguished from the others, i.e. bacteria and eukaryotes. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase, which catalyzes the transfer of a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate, is involved in the biosynthesis of archaeal membrane lipids. Enzymes of the UbiA prenyltransferase family are known to catalyze the transfer of a prenyl group to various acceptors with hydrophobic ring structures in the biosynthesis of respiratory quinones, hemes, chlorophylls, vitamin E, and shikonin. The thermoacidophilic archaeon Sulfolobus solfataricus was found to encode three homologues of UbiA prenyltransferase in its genome. One of the homologues encoded by SSO0583 was expressed in Escherichia coli, purified, and characterized. Radio-assay and mass spectrometry analysis data indicated that the enzyme specifically catalyzes the biosynthesis of (S)-2,3-di-O-geranylgeranylglyceryl phosphate. The fact that the orthologues of the enzyme are encoded in almost all archaeal genomes clearly indicates the importance of their functions. A phylogenetic tree constructed using the amino acid sequences of some typical members of the UbiA prenyltransferase family and their homologues from S. solfataricus suggests that the two other S. solfataricus homologues, excluding the (S)-2,3-di-Ogeranylgeranylglyceryl phosphate synthase, are involved in the production of respiratory quinone and heme, respectively. We propose here that archaeal prenyltransferases involved in membrane lipid biosynthesis might be prototypes of the protein family and that archaea might have played an important role in the molecular evolution of prenyltransferases.The structures of membrane lipids have some interesting and remarkable properties that enable us to distinguish archaea from other organisms, i.e. eukaryotes and bacteria (1) (Fig. 1). Although the archaeal "diether" membrane lipids are homologues of glycerolipids in other organisms, they differ with respect to the following features: 1) The hydrocarbon moieties of the archaeal lipids are fully reduced C 20 or C 25 prenyl groups, whereas the ordinary glycerolipids contain linear acyl groups. 2) The alkyl groups are attached to glycerol via an ether bond in archaeal lipids, while glycerol and the acyl chains are ester-bonded in the bacterial and eukaryotic glycerolipids.3) The two groups of membrane lipids have opposite chiralities at their glycerol moieties; in short, the glycerol moieties of the archaeal and other glycerolipids are sn-2,3-di-O-alkylated and sn-1,2-di-O-acylated, respectively. Moreover, the existence of circular "tetraether" lipids, which are synthesized from two molecules of diether lipids in methanogenic and thermophilic archaea, emphasizes the uniqueness of the archaeal membrane lipids.The biosynthesis of the core structure of archaeal membrane lipids has been studied to date (Fig. 2). The genes of (all-E) geranylgeranyl diphos...

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“…White or blue light strongly inhibits shikonin production by suppressing the gene expression of PHB geranyltransferase, a key enzyme in shikonin biosynthesis, 41,42) as well as 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, an enzyme responsible for the formation of the geranyl side chain of shikonin. 43) As shown in Fig.…”

Section: ϫmentioning

confidence: 99%

Regulation of Lithospermic Acid B and Shikonin Production in Lithospermum erythrorhizon Cell Suspension Cultures.

Yamamoto

Zhao

Yazaki

et al. 2002

CHEMICAL & PHARMACEUTICAL BULLETIN

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Caffeic acid oligomers such as rosmarinic acid and lithospermic acid B (LAB) are distributed in plants of Labiatae and Boraginaceae. Among these oligomers, LAB, the caffeic acid tetramer, has a variety of attractive pharmacological activities such as antioxidant and radical scavenging, 1,2) improvement of renal disease, [3][4][5][6] hypotensive, [7][8][9] improvement of myocardial infarction, 1,10) amplification of beating of myocardial muscles, 11) anti-hepatitis, 12) and aldose reductase inhibitory activity. 13) To utilize LAB as a medicinal resource, more than 30 plant sources were surveyed and only two medicinal plants, Salvia officinalis and Lithospermum erythrorhizon SIEB. et ZUCC, were found to contain this substance in an appreciable amount.14) Many attempts to produce this compound in high quantities using cell or hairy root cultures have been unsuccessful. [15][16][17][18][19][20][21][22] Recently, we found that L. erythrorhizon cell-suspension cultures, which were established for the industrial production of shikonin, 23) produced four caffeic acid oligomers, rosmarinic acid, LAB, a monoglucoside of LAB, and (ϩ)-rabdosiin. 24) In particular, the production of LAB in the cultured cells was highly stimulated in shikonin production medium M-9, 25) reaching almost the same amount as that of shikonin (LAB: ca. 6-10% of dry wt, and total shikonin derivatives: ca. 6-12% of dry wt.). 24,26) Since both LAB and shikonin are formed through a common phenylpropanoid pathway (Chart 1), the counterbalance between two metabolic routes either to LAB or to shikonin would be regulated in L. erythrorhizon cells, suggesting that the selection of suitable regulatory factors would result in higher production of LAB. However, the metabolic linkage and the regulatory mechanism for the biosyntheses of phenylpropanoid-derived compounds of diverse types in L. erythrorhizon cell cultures remain to be clarified. In this study, we investigated the critical regulatory factors to control these two biosynthetic pathways separately and to produce LAB efficiently in the culture system of L. erythrorhizon. ExperimentalCell Cultures The culture strain M18TOM 24) of Lithospermum erythrorhizon, which had been maintained in Linsmaier-Skoog (LS) medium 27) containing IAA 1 mM and kinetin 10 mM, was used in the present study. Cellsuspension cultures in 100-ml flasks each containing 30 ml of medium were agitated on a rotary shaker (80 rpm) at 23°C in the dark and subcultured at intervals of 2 weeks. The cells cultured in LS medium for 2 weeks were inoculated into M-9 medium, 25) modified M-9 or LS media containing 3% sucrose, and the same growth regulators as above (inoculum size: 1 g of fresh cells/30 ml of medium in a 100-ml flask) and cultured for 3 weeks under the above-mentioned culture conditions. For the investigation of the effect of light color on the production of secondary metabolites, each flask was covered with a commercially available colored cellophane sheet, 28) and irradiated with white light (10000 lx) from fluorescent lamps d...

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4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon : purification of a plant membrane-bound prenyltransferase

Cited by 45 publications

References 34 publications

The Role of Octadecanoids and Functional Mimics in Soybean Defense Responses

The Role of Octadecanoids and Functional Mimics in Soybean Defense Responses

(S)-2,3-Di-O-geranylgeranylglyceryl Phosphate Synthase from the Thermoacidophilic Archaeon Sulfolobus solfataricus

Regulation of Lithospermic Acid B and Shikonin Production in Lithospermum erythrorhizon Cell Suspension Cultures.

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