116 lines
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116 lines
12 KiB
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@prefix rdf: <http://www.w3.org/1999/02/22-rdf-syntax-ns#> .
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@prefix rdfs: <http://www.w3.org/2000/01/rdf-schema#> .
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<http://treatment.plazi.org/id/0397C353FFD8FFC0AA61FA8181F7FD69>
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cito:cites <http://dx.doi.org/10.5281/zenodo.10488181>, <http://dx.doi.org/10.5281/zenodo.10488178>, <http://dx.doi.org/10.5281/zenodo.10488184>, <http://dx.doi.org/10.5281/zenodo.10488188>, <http://dx.doi.org/10.5281/zenodo.10488190>, <http://dx.doi.org/10.5281/zenodo.10488193>, <http://dx.doi.org/10.5281/zenodo.10488195> ;
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dc:creator "Roepke, Jonathon; Bozzo, Gale G." ;
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dc:title "Arabidopsis" ;
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trt:publishedIn <http://dx.doi.org/10.1016/j.phytochem.2014.10.028> ;
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trt:treatsTaxonName <http://taxon-name.plazi.org/id/Plantae/Arabidopsis> ;
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a trt:Treatment .
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<http://dx.doi.org/10.1016/j.phytochem.2014.10.028>
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bibo:endPage "24" ;
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bibo:journal "Phytochemistry" ;
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bibo:pubDate "2015-01-31" ;
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bibo:startPage "14" ;
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bibo:volume "109" ;
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dc:creator "Roepke, Jonathon; Bozzo, Gale G." ;
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dc:date "2015" ;
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dc:title "Arabidopsis thaliana β-glucosidase BGLU 15 attacks flavonol 3 - O-β-glucoside- 7 - O- - rhamnosides" ;
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fabio:hasPart <http://dx.doi.org/10.5281/zenodo.10488181>, <http://dx.doi.org/10.5281/zenodo.10488178>, <http://dx.doi.org/10.5281/zenodo.10488184>, <http://dx.doi.org/10.5281/zenodo.10488188>, <http://dx.doi.org/10.5281/zenodo.10488190>, <http://dx.doi.org/10.5281/zenodo.10488193>, <http://dx.doi.org/10.5281/zenodo.10488195> ;
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a fabio:JournalArticle .
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<http://taxon-name.plazi.org/id/Plantae/Arabidopsis>
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dwc:class "Magnoliopsida" ;
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dwc:family "Brassicaceae" ;
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dwc:genus "Arabidopsis" ;
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dwc:kingdom "Plantae" ;
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dwc:order "Brassicales" ;
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dwc:phylum "Tracheophyta" ;
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dwc:kingdom "Plantae" ;
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dwc:order "Brassicales" ;
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dwc:kingdom "Plantae" ;
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dwc:kingdom "Plantae" ;
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a dwcFP:TaxonName .
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<http://dx.doi.org/10.5281/zenodo.10488181>
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dc:description "Fig. 2. Evidence for Q3G7R (2) hydrolyzing activity from cell-free Arabidopsis extracts is coincident with the loss of flavonol 3-O-β-glucoside-7-O-α-rhamnosides during synergistic abiotic stress recovery. (A) Plants were maintained under 0 mM nitrate at 10 °C (nitrogen deficiency and low temperature, NDLT; represented as the grey-shaded portion of the time course) for 7 days. Thereafter plants were repleted with 10 mM nitrate and maintained at 21 °C (nitrogen sufficiency and high temperature, NSHT; represented as the non-shaded portion of the time course) for 5 days. (B) As a control, plants of similar age were left under continual NSHT. K3G7R (1) and Q3G7R (2) concentrations were determined by UHPLC-DAD-MS n analysis of acidified methanolic extracts. A peak areas for Q3G7R (2; retention time = 16.3 min) and K3G7R 360 (retention time = 16.9 min) were compared to known amounts of Q3G and corrected for amount of fresh matter used for the extraction.MS n analysis confirmed the identity of K3G7R (1) with an [M—H] —1 parent ion of 593.2 and fragment ions of 447.2, 431.2 and 285.1; Q3G7R (2) analysis revealed a parent ion of 609.2 and fragment ions of 463.2, 447.2 and 301.1. Q3G7R (2) hydrolysis rate reflects the amount of product formed following 5 h incubation with Arabidopsis enzyme preparations using assay A and their analysis by HPLC-DAD (see Experimental). Reaction rates are expressed as pmol quercetin equivalents min—1 mg protein—1. For all plots, each data point represents the mean ± SE of three separate experiments." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488181/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10488178>
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dc:description "Fig. 1. Hydrolysis of kaempferol 3-O-β-glucoside-7-O-α-rhamnoside (1) and quercetin 3-O-β-glucoside-7-O-α-rhamnoside (2) by β-glucosidase from Arabidopsis thaliana yielding kaempferol 7-O-α-rhamnoside (3) and quercetin 7-O-α-rhamnoside (4)." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488178/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10488184>
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dc:description "Fig. 3. Quercetin 3-O-β-glucoside-7-O-α-rhamnoside β-glucosidase activity in crude protein extracts obtained from Arabidopsis plants growing under NDLT for 7 days and NSHT for 2 days. (A) HPLC-DAD analysis of enzyme assay shows the formation of a reaction product (P) with the retention time 13.3 min. The reaction product (see magnification in the inset) was produced in the presence of the protein extract (grey line) but not in its absence (black line) (B) Analysis of the purified reaction product by negative ion quadrupole TOF-MS/MS produced a molecular mass of 448.2." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488184/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10488188>
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dc:description "Fig. 4. Phylogenetic tree of amino acid sequences of Arabidopsis and other plant glycoside hydrolase family 1 BGLUs. The unrooted tree was constructed with maximum likelihood method in MEGA 6.06 (Tamura et al., 2013), following multiple protein sequence alignment with ClustalW (www.genome.jp/tools/clustalw; Larkin et al., 2007). The numbers shown at each node of the tree are representative of percent support values greater than 60 obtained by bootstrap analysis using 1000 replicates. BGLUs shown in black represent biochemically and/or functionally characterized enzymes; BGLUs shown in grey represent enzymes not yet biochemically characterized. Biochemically characterized flavonoid glycoside utilizing enzymes and are represented in blue. Arabidopsis (displayed in red font) and rice (Oryza sativa, Os) amino acid sequences are as designated by Xu et al. (2004) and Opassiri et al. (2006), respectively; where applicable, their biochemical function is provided in square brackets.For amino acid sequences of BGLUs from other plant species used for the alignment, their corresponding GenBank™ accession numbers are provided in parentheses as follows: isoflavone conjugatehydrolyzing BGLU (Glycine max, BAF34333); non-cyanogenic BGLU (Cicer arietinum, CAG14979); linamarase (Trifolium repens, CAA40058); BGLU G1 (M. truncatula, ABW76286); BGLU G2 (M. truncatula, ABW76287); BGLU G3 (M. truncatula, ABW76288); BGLU G4 (M. truncatula, ABW76289); prunasin hydrolase (Prunus serotina, AAF34650); amygdalin hydrolase (Prunus serotina, AAA93234); furostanol glycoside 26-O-β-glucosidase (Cheilocostus speciosus, BAA11831); furcatin hydrolase (Viburnum furcatum, BAD14925); β-primeverosidase (Camellia sinensis, BAC78656); dalcochinin 80-O-β-glucoside BGLU (Dalbergia cochinchinensis, AAF04007); linamarase (Manihot esculenta, AAB22162); alkaloid BGLU (Carapichea ipecacuanha, BAH02544); raucaffricine BGLU (Rauvolfia serpentina, AAF03675); strictosidine BGLU (Rauvolfia serpentina, CAC83098); cardenolide 16-O-glucohydrolase (Digitalis lanata, CAB38854); myrosinase (Brassica napus, CAA42775); myrosinase (Raphanus sativus, BAB17226); thioglucoside glucohydrolase (Sinapis alba; CAA42534); coniferin β-glucosidase (Pinus contorta, AAC69619); dhurrinase (Sorghum bicolour, AAC49177); cytokinin glucoside β-glucosidase (Zea mays, CAA52293); β-glucosidase (Secale cereale, AAG00614); avenacosidase (Avena sativa, AAD02839); β-glucosidase (Hordeum vulgare, AAA87339); hydroxynitrile glucoside-cleaving β-glucosidase D2 (Lotus japonicus, ACD65510); hydroxynitrile glucoside-cleaving β-glucosidase D4 (L. japonicus, ACD65509); hydroxynitrile glucosidecleaving β-glucosidase D7 (L. japonicus, ACD65511). Accessions numbers for re-annotated amino acid sequences of putative M. truncatula BGLUs described by Suzuki et al. (2006) are as follows (ascribed a lower case for putative gene with similar names): M. truncatula BGLU D2a (AES76414); M. truncatula BGLU D2b (XP_003597509); M. truncatula BGLU D4a (XP_003620203); M. truncatula BGLU D4b (AES67734); M. truncatula BGLU D4c (XP_003589430); M. truncatula BGLU (AES67732).The bar at the bottom of the diagram represents the scale (0.2 substitutions per site) implemented to draw the branches." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488188/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10488190>
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dc:description "Fig. 5. Analysis of relative Arabidopsis BGLUs expression patterns. Plants were maintained under 0 mM nitrate at 10 °C (nitrogen deficiency and low temperature, NDLT; represented as the grey-shaded portion of the time course) for 7 days. Thereafter, plants were repleted with 10 mM nitrate and transferred to 21 °C (nitrogen sufficiency and high temperature, NSHT; represented as the non-shaded portion of the time course) for 5 days. Expression levels were determined by RTqPCR as indicated under Materials and Methods. For each BGLU gene, data is expressed as the fold change in NDLT treatments (before and after transfer to NSHT) relative to control (continuous NSHT) conditions (2 —ΔΔC). For each experimental T replicate, RT-qPCR reactions were performed in duplicate. For each time course data represents the mean ± SE of three separate experiments." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488190/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10488193>
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dc:description "Fig. 6. SDS–PAGE (A) and immunoblot analysis (B) of the expression and purification of the mature recombinant BGLU15 from E. coli Origami 2 (DE3) cells. The left-hand lane on each gel contains the size in kDa of molecular mass standards. Each lane was loaded with 5 µL of the sample mixed with 5 µL of 2× sample dye. The immunoblot was probed with an anti-His6 antibody." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488193/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10488195>
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dc:description "Fig. 7. Relative substrate utilization of recombinant BGLU15. For each substrate, in vitro activity was measured at 500 µM using Assay B; each assays were incubated for 10 min and products detected by HPLC-DAD. Reaction rates are expressed as percentage of that calculated for K3G7R (1) (100% = 0.96 µmol min—1 mg protein —1) ± SE of three separate recombinant protein preparations." ;
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fabio:hasRepresentation <https://zenodo.org/record/10488195/files/figure.png> ;
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a fabio:Figure .
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