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Functional genomics of O-glucosyltra...

Brock University (Canada).

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Functional genomics of O-glucosyltransferases from Concord grape (Vitis labrusca).

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Functional genomics of O-glucosyltransferases from Concord grape (Vitis labrusca)./
Author:	Hall, Dawn.
Description:	223 p.
Notes:	Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 7813.
Contained By:	Dissertation Abstracts International68-12B.
Subject:	Agriculture, Plant Culture. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR35501
ISBN:	9780494355015

Functional genomics of O-glucosyltransferases from Concord grape (Vitis labrusca).
Hall, Dawn.

Functional genomics of O-glucosyltransferases from Concord grape (Vitis labrusca). - 223 p.

Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 7813.

Thesis (Ph.D.)--Brock University (Canada), 2007.

Grape (Vitis spp.) is a culturally and economically important crop plant that has been cultivated for thousands of years, primarily for the production of wine. Grape berries accumulate a myriad of phenylpropanoid secondary metabolites, many of which are glucosylated in planta. More than 90 O-glucosyltransferases have been cloned and biochemically characterized from plants, only two of which have been isolated from Vitis spp. The world-wide economic importance of grapes as a crop plant, the human health benefits associated with increased consumption of grape-derived metabolites, the biological relevance of glucosylation, and the lack of information about Vitis glucosyltransferases has inspired the identification, cloning and biochemical characterization of five novel "family 1" O-glucosyltransferases from Concord grape (Vitis labrusca cv. Concord).

ISBN: 9780494355015Subjects--Topical Terms:

1018669
Agriculture, Plant Culture.

Functional genomics of O-glucosyltransferases from Concord grape (Vitis labrusca).
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020 $a 9780494355015
035 $a (UMI)AAINR35501
035 $a AAINR35501
040 $a UMI $c UMI
100 1 $a Hall, Dawn. $3 1018668
245 1 0 $a Functional genomics of O-glucosyltransferases from Concord grape (Vitis labrusca).
300 $a 223 p.
500 $a Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 7813.
502 $a Thesis (Ph.D.)--Brock University (Canada), 2007.
520 $a Grape (Vitis spp.) is a culturally and economically important crop plant that has been cultivated for thousands of years, primarily for the production of wine. Grape berries accumulate a myriad of phenylpropanoid secondary metabolites, many of which are glucosylated in planta. More than 90 O-glucosyltransferases have been cloned and biochemically characterized from plants, only two of which have been isolated from Vitis spp. The world-wide economic importance of grapes as a crop plant, the human health benefits associated with increased consumption of grape-derived metabolites, the biological relevance of glucosylation, and the lack of information about Vitis glucosyltransferases has inspired the identification, cloning and biochemical characterization of five novel "family 1" O-glucosyltransferases from Concord grape (Vitis labrusca cv. Concord).
520 $a Protein purification and associated protein sequencing led to the molecular cloning of UDP-glucose: resveratrol/hydroxycinnamic acid O-glucosyltransferase (VLRSGT) from Vitis labrusca berry mesocarp tissue. In addition to being the first glucosyltransferase which accepts trans-resveratrol as a substrate to be characterized in vitro, the recombinant VLRSGT preferentially produces the glucose esters of hydroxycinnamic acids at pH 6.0, and the glucosides of trans-resveratrol and flavonols at pH 9.0; the first demonstration of pH-dependent bifunctional glucosylation for this class of enzymes. Gene expression and metabolite profiling support a role for this enzyme in the bifuncitonal glucosylation of stilbenes and hydroxycinnamic acids in planta.
520 $a A homology-based approach to cloning was used to identify three enzymes from the Vitis vinifera TIGR grape gene index which had high levels of protein sequence identity to previously characterized UDP-glucose: anthocyanin 5-O-glucosyltransferases. Molecular cloning and biochemical characterization demonstrated that these enzymes (rVLOGT1, rVLOGT2, rVLOGT3) glucosylate the 7-O-position of flavonols and the xenobiotic 2,4,5-trichlorophenol (TCP), but not anthocyanins. Variable gene expression throughout grape berry development and enzyme assays with native grape berry protein are consistent with a role for these enzymes in the glucosylation of flavonols; while the broad substrate specificity, the ability of these enzymes to glucosylate TCP and expression of these genes in tissues which are subject to pathogen attack (berry, flower, bud) is consistent with a role for these genes in the plant defense response.
520 $a Additionally, the Vitis labrusca UDP-glucose: flavonoid 3-O-glueosyltransferase (VL3GT) was identified, cloned and characterized. VL3GT has 96% protein sequence identity to the previously characterized Vitis vinifera flavonoid 3-O-glucosyltransferase (VV3GT); and glucosylates the 3-O-position of anthocyanidins and flavonols in vitro. Despite high levels of protein sequence identity, VL3GT has distinct biochemical characteristics (as compared to VV3GT), including a preference for B-ring methylated flavonoids and the inability to use UDP-galactose as a donor substrate. RT-PCR analysis of VL3GT gene expression and enzyme assays with native grape protein is consistent with an in planta role for this enzyme in the glucosylation of anthocyanidins, but not flavonols.
520 $a These studies reveal the power of combining several biochemistry- and molecular biology-based tools to identify, clone, biochemically characterize and elucidate the in planta function of several biologically relevant O-glucosyltransferases from Vitis spp.
590 $a School code: 1476.
650 4 $a Agriculture, Plant Culture. $3 1018669
650 4 $a Biology, Molecular. $3 1017719
690 $a 0307
690 $a 0479
710 2 $a Brock University (Canada). $3 1018667
773 0 $t Dissertation Abstracts International $g 68-12B.
790 $a 1476
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR35501