Uptake of isopentenyl diphosphate by plastids isolated from Vitis vinifera L. cell suspensions

Soler, E.; Clastre, Marc; Bantignies, Brigitte; Marigo, G.; Ambid, Christian

doi:10.1007/bf00195689

Cited by 48 publications

(32 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…13), the cross-talk between both pathways might also be regulated by the circadian clock (54) and environmental stress (17). There are complementary results showing the capability of plastids to import (52,53,(55)(56)(57)(58) as well as to export IPP (59,60).…”

mentioning

confidence: 51%

Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Dolichols in Plants

Skorupińska-Tudek

Poznański

Wójcik

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

Plant isoprenoids are derived from two biosynthetic pathways, the cytoplasmic mevalonate (MVA) and the plastidial methylerythritol phosphate (MEP) pathway. In this study their respective contributions toward formation of dolichols in Coluria geoides hairy root culture were estimated using in vivo labeling with 13 C-labeled glucose as a general precursor. NMR and mass spectrometry showed that both the MVA and MEP pathways were the sources of isopentenyl diphosphate incorporated into polyisoprenoid chains. The involvement of the MEP pathway was found to be substantial at the initiation stage of dolichol chain synthesis, but it was virtually nil at the terminal steps; statistically, 6 -8 isoprene units within the dolichol molecule (i.e. 40 -50% of the total) were derived from the MEP pathway. These results were further verified by incorporation of Polyisoprenoid alcohols together with sterols and quinone side chains constitute three main branches of terpene products originating from farnesyl diphosphate (FPP) 4 (1). These linear five-carbon unit polymers are divided into two groups, i.e. polyprenols and dolichols, according to the hydrogenation status of the ␣-terminal isoprene unit (dolichol structure is shown in Fig. 1). In cells, polyprenols and dolichols are always found as mixtures of prenologues, and data collected so far show polyprenols to be typical for bacteria and plants, whereas dolichols are generally attributed to animals and yeast (2). Nevertheless, it should be remembered that dolichols are the predominant form in some plant organs like roots (3). Data on the occurrence and functions of polyisoprenoids are summarized in recently published reviews (4, 5). The formation of the polyisoprenoid chain, starting from the -end of the molecule (Fig. 1), proceeds in a biphasic manner with farnesyl-diphosphate synthase responsible for the synthesis of the all-trans-FPP (three isoprene units of -t 2 structure, t stands for trans-isoprene unit), and its further elongation by cis-prenyltransferase. The latter enzyme, cloned from several prokaryotic and eukaryotic organisms (see Refs. 6, 7 and references therein), including Arabidopsis thaliana (8,9) and Hevea brasiliensis (10), utilizes isopentenyl diphosphate (IPP) for elongation of FPP up to the desired chain length, thus producing a family of polyprenyl diphosphates (n isoprene units of -t 2 -c n-3 structure, c stands for cis-isoprene unit), which are subsequently converted to polyprenols or dolichols according to the "tissue-specific requirements" by a still unknown mechanism.In plant cells two pathways are known to produce IPP utilized by numerous enzymes to finally give more than 50,000 different isoprenoid structures, the mevalonate pathway (MVA) and the mevalonate-independent methylerythritol phosphate pathway (MEP) (for reviews, see Refs. 11-13). Both pathways are compartmentalized as follows: the MVA in the cytoplasm to provide sterols, the many sesquiterpenes, and the prenyl chains of ubiquinones, and the MEP one in the plastids Tables 1 and 2

show abstract

mentioning

confidence: 51%

Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Dolichols in Plants

Skorupińska-Tudek

Poznański

Wójcik

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…For example, IPP import into mitochondria (Lü tke-Brinkhaus et al, 1984) and exchange of IPP between the cytosol and plastid have been documented by inhibitor studies in Arabidopsis (Laule et al, 2003) and in vivo feeding studies in several plant systems, including tobacco BY-2 cultures (Hemmerlin et al, 2003), snapdragon (Antirrhinum majus) (Dudareva et al, 2005), chamomile (Chamaemelum nobile) (Adam et al, 1999), and lima bean (Phaseolus lunatus) (Piel et al, 1998). In vitro studies with isolated membranes also support the transport of IPP from plastids to the cytosol (and possibly DMAPP, albeit at very low levels) (Bick and Lange, 2003) and from the cytosol to plastids (Kreuz and Kleinig, 1984;Soler et al, 1993;Flü gge and Gao, 2005). Among earlier isoprenoid intermediates, exogenously supplied mevalonate, an intermediate in the cytosolic IPP pathway, has been shown to partially rescue a block in the plastidic MEP pathway (Esté vez et al, 2000;Nagata et al, 2002;Gutié rrez-Nava et al, 2004;Rodríguez-Concepció n et al, 2004).…”

Section: Single Mutants In Idi1 or Idi2 Are Rescued By The Remaining Idimentioning

confidence: 93%

The Arabidopsis thaliana Type I Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have Overlapping Functions in Isoprenoid Biosynthesis

et al. 2008

View full text Add to dashboard Cite

To form the building blocks of isoprenoids, isopentenyl diphosphate (IPP) isomerase activity, which converts IPP to dimethylallyl diphosphate (DMAPP), appears to be necessary in cytosol, plastids, and mitochondria. Arabidopsis thaliana contains only two IPP isomerases (Isopentenyl Diphosphate Isomerase1 [IDI1] and IDI2). Both encode proteins with N-terminal extensions similar to transit peptides and are expressed in all organs, with IDI1 less abundant than IDI2. Examination of enhanced green fluorescent protein fusions established that IDI1 is mainly in the plastid, whereas IDI2 is mainly in the mitochondria. Both proteins are also in the cytosol as a result of their translation from naturally occurring shorter transcripts lacking transit peptides, as demonstrated by 59 rapid amplification of cDNA ends cloning. IPP isomerase activity in the cytosol was confirmed by uniform labeling of IPP-and DMAPP-derived units of the cytoplasmic isoprenoid product, sitosterol, when labeled mevalonate was administered. Analysis of mutant lines showed that double mutants were nonviable, while homozygous single mutants had no major morphological or chemical differences from the wild type except for flowers with fused sepals and underdeveloped petals on idi2 mutants. Thus, each of the two Arabidopsis IPP isomerases is found in multiple but partially overlapping subcellular locations, and each can compensate for the loss of the other through partial redundancy in the cytosol.

show abstract

“…IPP, DMAPP, or geranylgeranyl diphosphate) responsible for the crossover between two isoprenoid pathways needs to be determined. An active uptake of IPP into isolated plastids in a facilitated-diffusion manner (43)(44)(45) implies that IPP may be involved in the precursor exchange between the MVA and MEP pathways.…”

Section: Discussionmentioning

confidence: 99%

Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Gibberellins inArabidopsis

Kasahara¹,

Hanada²,

Kuzuyama³

et al. 2002

Journal of Biological Chemistry

242

179

View full text Add to dashboard Cite

Gibberellins (GAs) are diterpene plant hormones essential for many developmental processes. Although the GA biosynthesis pathway has been well studied, our knowledge on its early stage is still limited. There are two possible routes for the biosynthesis of isoprenoids leading to GAs, the mevalonate (MVA) pathway in the cytosol and the methylerythritol phosphate (MEP) pathway in plastids. To distinguish these possibilities, metabolites from each isoprenoid pathway were selectively labeled with 13 C in Arabidopsis seedlings. Efficient 13 C-labeling was achieved by blocking the endogenous pathway chemically or genetically during the feed of a 13 C-labeled precursor specific to the MVA or MEP pathways. Gas chromatography-mass spectrometry analyses demonstrated that both MVA and MEP pathways can contribute to the biosyntheses of GAs and campesterol, a cytosolic sterol, in Arabidopsis seedlings. While GAs are predominantly synthesized through the MEP pathway, the MVA pathway plays a major role in the biosynthesis of campesterol. Consistent with some crossover between the two pathways, phenotypic defects caused by the block of the MVA and MEP pathways were partially rescued by exogenous application of the MEP and MVA precursors, respectively. We also provide evidence to suggest that the MVA pathway still contributes to GA biosynthesis when this pathway is limiting.

show abstract

Uptake of isopentenyl diphosphate by plastids isolated from Vitis vinifera L. cell suspensions

Cited by 48 publications

References 27 publications

Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Dolichols in Plants

Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Dolichols in Plants

The Arabidopsis thaliana Type I Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have Overlapping Functions in Isoprenoid Biosynthesis

Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Gibberellins inArabidopsis

Contact Info

Product

Resources

About