Determination of phytyl diphosphate and geranylgeranyl diphosphate in etiolated oat seedlings

Benz, Jürgen; Fischer, I.; Rüdiger, Wolfhart

doi:10.1016/s0031-9422(00)97700-8

Cited by 13 publications

(9 citation statements)

References 17 publications

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“…Ϫ1 reported for geranylgeranyl diphosphate and phytyl diphosphate, respectively, in etoliated oat leaves (31). The roughly 3.5-fold increase in our observed DMAPP levels in the light-adapted leaves is most likely due to an increased production of DMAPP in the chloroplasts in the light, for incorporation into higher isoprenoids, rather than increased metabolism of existing DMAPP in the dark.…”

Section: Figsupporting

confidence: 54%

Nonradioactive Assay for Cellular Dimethylallyl Diphosphate

Fisher

Rosenstiel

Shirk

et al. 2001

Analytical Biochemistry

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Section: Figsupporting

confidence: 54%

Nonradioactive Assay for Cellular Dimethylallyl Diphosphate

Fisher

Rosenstiel

Shirk

et al. 2001

Analytical Biochemistry

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“…This concentration is presumably higher than the physiological concentration in oat tissue which can be estimated roughly as follows: The biosynthetic pathway from MVA to GGPP comThe amount of GGPP has been estimated to be prises several enzymes (MVA-kinase, 5-P MVA kinase, 16 nmol/g fr. wt [17] which is nearly identical with the IPP isomerase, GGPP synthase). To determine whether protochlorophyllide content of 15 nmol/g fr.…”

Section: Resultsmentioning

confidence: 93%

“…The production of [14C]GGPP from [14C]MVA in the Cucurbita system was verified by isolation of GGPP by the method of Benz et al [17] which basically comprises five chromatographic steps. It was more convenient, however, to hydrolyse GGPP in the aqueous layer after preextraction of lipophilic compounds with diethylether and then determine free GG and GL (see Experimental).…”

Section: Resultsmentioning

confidence: 99%

“…PhPP and GGPP are very similar and therefore both are accepted by enzymes like chlorophyll synthetase [16]. GGPP is present in etiolated and green seedlings in about ten fold higher concentration than PhPP [ 17,181. The GGPP pool of etiolated oat seedlings which is depleted during onset of chlorophyll biosynthesis seems to be reestablished only to a well-defined limiting value [18].…”

Section: Introduchonmentioning

confidence: 99%

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Inhibition of geranylgeranyl diphosphate synthesis in in vitro systems

et al. 1985

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Abstract-The incorporation of [14C]mevalonate and ["Clisopentenyl diphosphate into geranylgeranyl diphosphate was investigated in in oitro systems from Cucurbita pepo (pumpkin) endosperm and from Auena sativa etioplasts. Mevalonate incorporation was effectively inhibited in the pumpkin system by geranylgeranyl diphosphate and geranylgeranyl monophosphate but less effectively by phytyl diphosphate or inorganic diphosphate. Membrane lipids, geranyllinalool, or lecithin enhanced mevalonate incorporation in the Cucurbita system. Incorporation of isopentenyl diphosphate was also enhanced by lecithin and inhibited by geranylgeranyl diphosphate in the Cucurbita system. NO lipid enhancement was found in the Auena system; inhibition by GGPP required a much higher GGPP concentration than in the Cucurbita system. INTRODUCHONThe biosynthesis of GGPP has received considerable attention be-cause it is the precursor of the biologically important diterpenes (e.g. gibbexellins, phytol side chain of chlorophylls, phylloquinone, tocopherol) and tetraterpenes (carotenoids). Systems for in vitro synthesis of GGPP have been described for various organisms [l-l 11. The biosynthetic pathway from MVA to GGPP is catalysed by several enzymes (MVA-kinase, 5-P MVA kinase, IPP isomerase, GG synthase) which are all soluble [2,6,8,10,12].The last enzyme (GG synthase) was purified from a bacterial [2] and a plant source [6]; it catalyses the reaction of IPP with either DMAPP, GPP or FPP to GGPP. In none of these papers was the regulation of GGPP biosynthesis studied.The biosynthesis of phytol which is closely connected to that of GGPP [ 133 is inhibited by PhPP [ 143. This effect is attributed to feed-back inhibition because it has been demonstrated that mevalonate kinase is inhibited by PhPP [lS]. PhPP and GGPP are very similar and therefore both are accepted by enzymes like chlorophyll synthetase [16]. GGPP is present in etiolated and green seedlings in about ten fold higher concentration than PhPP [ 17,181. The GGPP pool of etiolated oat seedlings which is depleted during onset of chlorophyll biosynthesis seems to be reestablished only to a well-defined limiting value [18]. In pumpkin endosperm, only a limited ac- In the study reported in this paper, we have investigated whether GGPP is able to regulate its own biosynthesis in in vitro systems from etiolated oat seedlings and from Cucurbita endosperm. RESULTSA cell-free system (35 KS) from the endosperm of immature seeds of C. pepo was able to convert MVA into several lipid compounds (Table 1). The product pattern shows that the bulk of isoprenoid lipids were derived from GGPP (kaurene, GG, carotenes) with only a small part of the lipids being derived from FPP (farnesol, squalene, sterols). In the presence of AM0 1618 the incorporation of MVA was strongly reduced. Although the lipid pattern was shifted by AM0 1618 towards the FPP products the larger part of the isoprenoid lipids were still derived from GGPP. It was to be expected, therefore, that GGPP rather than FPP was the main water-solub...

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“…The authors themselves (Ghirardo et al, 2010) recognized that their values might be overestimates of in planta GDP levels, since linalool might be formed from other substances under acidic conditions. For GGDP, 10-fold higher amounts in etiolated oat (Avena sativa) seedlings were reported (Benz et al, 1983). Large amounts of GGDP might be present in etiolated seedlings to form chlorophyll and initiate photosynthesis rapidly on illumination.…”

Section: Overexpression Of Ids1 Does Not Increase the Content Of Typimentioning

confidence: 98%

Overexpression of an Isoprenyl Diphosphate Synthase in Spruce Leads to Unexpected Terpene Diversion Products That Function in Plant Defense

et al. 2013

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Spruce (Picea spp.) and other conifers employ terpenoid-based oleoresin as part of their defense against herbivores and pathogens. The short-chain isoprenyl diphosphate synthases (IDS) are situated at critical branch points in terpene biosynthesis, producing the precursors of the different terpenoid classes. To determine the role of IDS and to create altered terpene phenotypes for assessing the defensive role of terpenoids, we overexpressed a bifunctional spruce IDS, a geranyl diphosphate and geranylgeranyl diphosphate synthase in white spruce (Picea glauca) saplings. While transcript level (350-fold), enzyme activity level (7-fold), and in planta geranyl diphosphate and geranylgeranyl diphosphate levels (4-to 8-fold) were significantly increased in the needles of transgenic plants, there was no increase in the major monoterpenes and diterpene acids of the resin and no change in primary isoprenoids, such as sterols, chlorophylls, and carotenoids. Instead, large amounts of geranylgeranyl fatty acid esters, known from various gymnosperm and angiosperm plant species, accumulated in needles and were shown to act defensively in reducing the performance of larvae of the nun moth (Lymantria monacha), a conifer pest in Eurasia. These results show the impact of overexpression of an IDS and the defensive role of an unexpected accumulation product of terpenoid biosynthesis with the potential for a broader function in plant protection.

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Determination of phytyl diphosphate and geranylgeranyl diphosphate in etiolated oat seedlings

Cited by 13 publications

References 17 publications

Nonradioactive Assay for Cellular Dimethylallyl Diphosphate

Nonradioactive Assay for Cellular Dimethylallyl Diphosphate

Inhibition of geranylgeranyl diphosphate synthesis in in vitro systems

Overexpression of an Isoprenyl Diphosphate Synthase in Spruce Leads to Unexpected Terpene Diversion Products That Function in Plant Defense

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