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Tytuł:
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Two flavonoid glucosyltransferases from Petunia hybrida: molecular cloning, biochemical properties and developmentally regulated expression.
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Autorzy:
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Yamazaki M; Laboratory of Molecular Biology and Biotechnology, Graduate School of Pharmaceutical Sciences, Chiba University, Japan.
Yamagishi E
Gong Z
Fukuchi-Mizutani M
Fukui Y
Tanaka Y
Kusumi T
Yamaguchi M
Saito K
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Źródło:
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Plant molecular biology [Plant Mol Biol] 2002 Mar; Vol. 48 (4), pp. 401-11.
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Typ publikacji:
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Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: Dordrecht : Kluwer Academic
Original Publication: The Hague ; Boston : Martinus Nijhoff/Dr. W. Junk, 1981-
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MeSH Terms:
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Glucosyltransferases/*genetics
Solanaceae/*genetics
Amino Acid Sequence ; Anthocyanins/biosynthesis ; Blotting, Northern ; Blotting, Southern ; Cloning, Molecular ; DNA, Complementary/chemistry ; DNA, Complementary/genetics ; DNA, Complementary/isolation & purification ; DNA, Plant/genetics ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Plant ; Glucosyltransferases/metabolism ; Molecular Sequence Data ; Phylogeny ; RNA, Plant/genetics ; RNA, Plant/metabolism ; Saccharomyces cerevisiae/genetics ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Solanaceae/enzymology ; Solanaceae/growth & development
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References:
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Substance Nomenclature:
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0 (Anthocyanins)
0 (DNA, Complementary)
0 (DNA, Plant)
0 (RNA, Plant)
EC 2.4.1.- (Glucosyltransferases)
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Entry Date(s):
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Date Created: 20020322 Date Completed: 20020328 Latest Revision: 20190822
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Update Code:
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20240104
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DOI:
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10.1023/a:1014043214943
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PMID:
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11905966
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Two flavonoid glucosyltransferases, UDP-glucose:flavonoid 3-0-glucosyltransferase (3-GT) and UDP-glucose: anthocyanin 5-O-glucosyltransferase (5-GT), are responsible for the glucosylation of anthocyani(di)ns to produce stable molecules in the anthocyanin biosynthetic pathway. The cDNAs encoding 3-GT and 5-GT were isolated from Petunia hybrida by hybridization screening with heterologous probes. The cDNA clones of 3-GT, PGT8, and 5-GT, PH1, encode putative polypeptides of 448 and 468 amino acids, respectively. A phylogenetic tree based on amino acid sequences of the family of glycosyltransferases from various plants shows that PGT8 belongs to the 3-GT subfamily and PH1 belongs to the 5-GT subfamily. The function of isolated cDNAs was identified by the catalytic activities for 3-GT and 5-GT exhibited by the recombinant proteins produced in yeast. The recombinant PGT8 protein could convert not only anthocyanidins but also flavonols into the corresponding 3-O-glucosides. In contrast, the recombinant PH1 protein exhibited a strict substrate specificity towards anthocyanidin 3-acylrutinoside, comparing with other 5-GTs from Perilla frutescens and Verbena hybrida, which showed broad substrate specificities towards several anthocyanidin 3-glucosides. The mRNA expression of both 3-GT and 5-GT increased in the early developmental stages of P. hybrida flower, reaching the maximum at the stage before flower opening. Southern blotting analysis of genomic DNA indicates that both 3-GT and 5-GT genes exist in two copies in P. hybrida, respectively. The results are discussed in relation to the molecular evolution of flavonoid glycosyltransferases.