The uptake of acylated anthocyanin into isolated vacuoles from a cell suspension culture of Daucus carota

Hopp, W.; Seitz, Hanns Ulrich

doi:10.1007/bf00392383

Cited by 97 publications

(62 citation statements)

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“…Klein et al (1996) reported the vacuolar transport of isovitexin, a flavone glucoside of barley, via an isovitexin/H ϩ antiport. Hopp and Seitz (1987) postulated that cyanidin glycosides acylated with sinapic acid were transported into carrot vacuoles by a high-affinity carrier, with a pH gradient across the tonoplast being involved in the uptake mechanism. The slight homology of TT12 with O-antigen and succinoglycan transporters may indicate that it has a preference for complex glycosylated substrates.…”

Section: The Tt12 Gene May Be Involved In Vacuolar Transport Of Flavomentioning

confidence: 99%

The TRANSPARENT TESTA12 Gene of Arabidopsis Encodes a Multidrug Secondary Transporter-like Protein Required for Flavonoid Sequestration in Vacuoles of the Seed Coat Endothelium

et al. 2001

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Phenolic compounds that are present in the testa interfere with the physiology of seed dormancy and germination. We isolated a recessive Arabidopsis mutant with pale brown seeds, transparent testa12 ( tt12 ), from a reduced seed dormancy screen. Microscopic analysis of tt12 developing and mature testas revealed a strong reduction of proanthocyanidin deposition in vacuoles of endothelial cells. Double mutants with tt12 and other testa pigmentation mutants were constructed, and their phenotypes confirmed that tt12 was affected at the level of the flavonoid biosynthetic pathway. The TT12 gene was cloned and found to encode a protein with similarity to prokaryotic and eukaryotic secondary transporters with 12 transmembrane segments, belonging to the MATE (multidrug and toxic compound extrusion) family. TT12 is expressed specifically in ovules and developing seeds. In situ hybridization localized its transcript in the endothelium layer, as expected from the effect of the tt12 mutation on testa flavonoid pigmentation. The phenotype of the mutant and the nature of the gene suggest that TT12 may control the vacuolar sequestration of flavonoids in the seed coat endothelium. INTRODUCTIONFlavonoids represent a highly diverse group of plant aromatic secondary metabolites. The major forms, which are anthocyanins (red to purple pigments), flavonols (colorless to pale yellow pigments), and proanthocyanidins (PAs), also known as condensed tannins (colorless pigments that brown with oxidation), are present in proportions and amounts that vary according to the plant species, the organ, the stage of development, and environmental growth conditions. Arabidopsis contains flavonoid pigments in vegetative tissues and in seeds (Shirley et al., 1995). In the mature testa, flavonoids were detected in both the endothelium and the three crushed parenchymal layers just above the endothelium . PAs have been shown to accumulate exclusively in the endothelium layer (Devic et al., 1999). Wild-type seed color depends on the stage of development: as long as the testa is transparent, until ‫ف‬ 10 days after pollination, the seed has the color of the underlying endosperm and embryo. At maturity, the testa becomes opaque after the oxidation of flavonoid pigments, which gives the seed its characteristic brown color. Therefore, the color of mutants with seed flavonoid defects ranges from pale yellow (complete lack of visible pigments in the testa) to pale brown, depending on the accumulated intermediate flavonoids .In Arabidopsis, mutants at 21 loci have been isolated on the basis of altered testa pigmentation (Figure 1). The genes disrupted in the transparent testa ( tt ) mutants tt3 , tt4 , tt5 , tt6 , and tt7 (Shirley et al., 1995) and the banyuls ( ban ) mutant (Albert et al., 1997) code for the enzymes dihydroflavonol-4-reductase (Shirley et al., 1992), chalcone synthase (Feinbaum and Ausubel, 1988), chalcone isomerase (Shirley et al., 1992), flavonol 3-hydroxylase (Pelletier and Shirley, 1996; Wisman et al., 1998), flavonol 3 Ј -hydroxylase (Ko...

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Section: The Tt12 Gene May Be Involved In Vacuolar Transport Of Flavomentioning

confidence: 99%

The TRANSPARENT TESTA12 Gene of Arabidopsis Encodes a Multidrug Secondary Transporter-like Protein Required for Flavonoid Sequestration in Vacuoles of the Seed Coat Endothelium

et al. 2001

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“…As in Daucus, the major anthocyanin in Arabidopsis is acylated with a sinapoyl moiety (Bloor and Abrahams, 2002), which may be added by a sinapoyl-Glc-utilizing SCPL protein. Further, since isolated Daucus vacuoles actively accumulate the sinapoylated anthocyanin, but not the nonacylated form, the sinapate moiety may function as a vacuolar uptake or retention tag (Hopp and Seitz, 1987). Alternatively, the sinapate moiety may be required for, or be the site of, glutathione derivatization by a glutathione S-transferase analogous to that encoded by the maize Bronze2 gene (Marrs et al, 1995).…”

Section: Candidate Reactions For Scpl Acyltransferases Can Be Found Tmentioning

confidence: 99%

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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The Arabidopsis (Arabidopsis thaliana) genome encodes a family of 51 proteins that are homologous to known serine carboxypeptidases. Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided into several major clades. The first group consists of 21 proteins which, despite the function implied by their annotation, includes two that have been shown to function as acyltransferases in plant secondary metabolism: sinapoylglucose:malate sinapoyltransferase and sinapoylglucose:choline sinapoyltransferase. A second group comprises 25 SCPL proteins whose biochemical functions have not been clearly defined. Genes encoding representatives from both of these clades can be found in many plants, but have not yet been identified in other phyla. In contrast, the remaining SCPL proteins include five members that are similar to serine carboxypeptidases from a variety of organisms, including fungi and animals. Reverse transcription PCR results suggest that some SCPL genes are expressed in a highly tissue-specific fashion, whereas others are transcribed in a wide range of tissue types. Taken together, these data suggest that the Arabidopsis SCPL gene family encodes a diverse group of enzymes whose functions are likely to extend beyond protein degradation and processing to include activities such as the production of secondary metabolites.Serine carboxypeptidases (SCPs) are members of the a/b hydrolase family of proteins, which make use of a Ser-Asp-His catalytic triad to cleave the carboxyterminal peptide bonds of their protein or peptide substrates (Hayashi et al., 1973(Hayashi et al., , 1975Bech and Breddam, 1989;Liao and Remington, 1990;Liao et al., 1992;Ollis et al., 1992). Proteins that contain this catalytic triad and are otherwise homologous to SCPs have been found in a variety of organisms (Doi et al., 1980;Kim and Hayashi, 1983;Breddam, 1986;Baulcombe et al., 1987;Galjart et al., 1988;Bradley, 1992;Degan et al., 1994;Endrizzi et al., 1994;Wajant et al., 1994;Jones et al., 1996;Li and Steffens, 2000). Many of these serine carboxypeptidase-like (SCPL) proteins have been annotated as peptidases based only on this shared sequence similarity; however, studies have shown that some of them function not as peptidases, but as acyltransferases and lyases (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000;Shirley et al., 2001). For example, several SCPL proteins have been shown to catalyze the production of plant secondary metabolites involved in herbivory defense and UV protection (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000), including the hydroxynitrile lyase from Sorghum bicolor (SbHNL) necessary for cyanogenesis, and the acyltransferases in wild tomato (Lycopersicon pennellii) that catalyze the formation 2,3,4-isobutyryl-Glc (Wajant et al., 1994;Lehfeldt et al., 2000). Two enzymes in Arabidopsis (Arabidopsis thaliana) responsible for sinapate ester biosynthesis are also SCPL proteins. Sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the formation of s...

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“…Because it is known that several herbicides, chloroacetanilides primarily, are targeted to the vacuole by glutathionation (Hopp and Seitz, 1987;Martinoia et al, 2001), it was of interest to know if the same would hold true for CS and, if so, whether the corresponding glutathione conjugate is transported by the same carrier as CSG. To examine this directly, we attempted to conjugate glutathione to CSOH but were unsuccessful.…”

Section: Glutathionation Of Ce Is a Prerequisite For Transportmentioning

confidence: 99%

“…Although uptake usually requires an energy source, for instance ATP, and occurs against a concentration gradient, the elucidation of general principles has been confounded by the paucity of systematic investigations and the seeming dependence of the energetics and kinetics of uptake not only on the identity of the Glc conjugate but also on the plant species from which the vacuoles were isolated. Another complicating factor is that there are examples of Glc conjugates that cannot enter the vacuole unless they are further modified, for instance by acylation (Matern et al, 1986;Hopp and Seitz, 1987;Wink, 1997). This is the case for apigenin 7-Oglucoside (the major pigment in parsley), which is conjugated to malonic acid before vacuolar transport (Matern et al, 1986).…”

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confidence: 99%

Alternate Energy-Dependent Pathways for the Vacuolar Uptake of Glucose and Glutathione Conjugates

et al. 2002

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Through the development and application of a liquid chromatography-mass spectrometry-based procedure for measuring the transport of complex organic molecules by vacuolar membrane vesicles in vitro, it is shown that the mechanism of uptake of sulfonylurea herbicides is determined by the ligand, glucose, or glutathione, to which the herbicide is conjugated. ATP-dependent accumulation of glucosylated chlorsulfuron by vacuolar membrane vesicles purified from red beet (Beta vulgaris) storage root approximates Michaelis-Menten kinetics and is strongly inhibited by agents that collapse or prevent the formation of a transmembrane H+gradient, but is completely insensitive to the phosphoryl transition state analog, vanadate. In contrast, ATP-dependent accumulation of the glutathione conjugate of a chlorsulfuron analog, chlorimuron-ethyl, is incompletely inhibited by agents that dissipate the transmembrane H+ gradient but completely abolished by vanadate. In both cases, however, conjugation is essential for net uptake because neither of the unconjugated parent compounds are accumulated under energized or nonenergized conditions. That the attachment of glucose to two naturally occurring phenylpropanoids, p-hydroxycinnamic acid and p-hydroxybenzoic acid via aromatic hydroxyl groups, targets these compounds to the functional equivalent of the transporter responsible for chlorsulfuron-glucoside transport, confirms the general applicability of the H+ gradient dependence of glucoside uptake. It is concluded that H+gradient-dependent, vanadate-insensitive glucoside uptake is mediated by an H+ antiporter, whereas vanadate-sensitive glutathione conjugate uptake is mediated by an ATP-binding cassette transporter. In so doing, it is established that liquid chromatography-mass spectrometry affords a versatile high-sensitivity, high-fidelity technique for studies of the transport of complex organic molecules whose synthesis as radiolabeled derivatives is laborious and/or prohibitively expensive.

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The uptake of acylated anthocyanin into isolated vacuoles from a cell suspension culture of Daucus carota

Cited by 97 publications

References 62 publications

The TRANSPARENT TESTA12 Gene of Arabidopsis Encodes a Multidrug Secondary Transporter-like Protein Required for Flavonoid Sequestration in Vacuoles of the Seed Coat Endothelium

The TRANSPARENT TESTA12 Gene of Arabidopsis Encodes a Multidrug Secondary Transporter-like Protein Required for Flavonoid Sequestration in Vacuoles of the Seed Coat Endothelium

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

Alternate Energy-Dependent Pathways for the Vacuolar Uptake of Glucose and Glutathione Conjugates

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