Genetic sequences encoding glycosyltransferase enzymes and uses

Details Genetic sequences encoding glycosyltransferase enzymes and uses Genetic sequences encoding glycosyltransferase enzymes and uses

1995-03-13

1999-01-12

Chereskin, Che S.

Multicellular living organisms and unmodified parts thereof and

Method of introducing a polynucleotide molecule into or...

The polynucleotide alters fat, fatty oil, ester-type wax, or...

800DIG67, 536 232, 536 243, 4353201, 4351723, A01H 400, C12N 1582, C12N 1529

Patent

active

058593349

DESCRIPTION:

BRIEF SUMMARY
The present invention relates generally to genetic sequences encoding flavonoid pathway metabolising enzymes and in particular flavonoid glycosylating enzymes and their use such as in manipulating production of pigmentory molecules in plants.
Bibliographic details of the publications referred to hereinafter in the specification are collected at the end of the description. SEQ ID No's referred to herein in relation to nucleotide and amino acid sequences are defined after the Bibliography.
The flower industry strives to develop new and different varieties of flowering plants. An effective way to create such novel varieties is through the manipulation of flower colour and classical breeding techniques have been used with some success to produce a wide range of colours for most of the commercial varieties of flowers. This approach has been limited, however, by the constraints of a particular species' gene pool and for this reason it is rare for a single species to have a full spectrum of coloured varieties. For example, the development of blue varieties of major cutflower species such as rose, chrysanthemum, tulip, lily, carnation and gerbera would offer a significant opportunity in both the cutflower and ornamental markets.
Flower colour is predominantly due to three types of pigment: flavonoids, carotenoids and betalains. Of the three the flavonoids are the most common and contribute a range of colours from yellow to red to blue. The flavonoid molecules which make the major contribution to flower colour are the anthocyanins which are glycosylated derivatives of cyanidin, delphinidin, petunidin, peonidin, malvidin and pelargonidin, and are localised in the vacuole.
The flavonoid pigments are secondary metabolites of the phenylpropanoid pathway. The biosynthetic pathway for the flavonoid pigments ("flavonoid pathway") is well established. (Ebel and Hahlbrock. 1988; Hahlbrock and Grisebach. 1979: Wiering and De Vlaming, 1984: Schram et al., 1984; Stafford. 1990) and is shown in FIGS. 1A and B. Three reactions and enzymes are involved in the conversion of phenylalanine to p-coumaroyl-CoA, one of the first key substrates in the flavonoid pathway. The enzymes are phenylalanine ammonia-lyase (PAL), cinnamate 4-hydroxylase (C4H) and 4-coumarate: CoA ligase (4CL). The first committed step in the pathway involves the condensation of three molecules of malonyl-CoA (provided by the action of acetyl CoA carboxylase (ACC) on acetyl CoA and CO.sub.2), with one molecule of p-coumaroyl-CoA. This reaction is catalysed by the enzyme chalcone synthase (CHS). The product of this reaction, 2', 4,4', 6', tetrahydroxy-chalcone, is normally rapidly isomerized by the enzyme chalcone flavanone isomerase (CHI) to produce naringenin. Naringenin is subsequently hydroxylated at the 3 position of the central ring by flavonol 3-hydroxylase (F3H) to produce dihydrokaempferol (DHK).
The B-ring of dihydrokaempterol can be hydroxylated at either the 3', or both the 3' and 5' positions, to produce dihydroquercetin (DHQ) and dihydromyricetin (DHM), respectively. The pattern of hydroxylation of the B-ring plays a key role in determining petal colour.
The dihydroflavonols (DHK, DHQ and DHM) can also be acted upon by flavonol synthase to produce the flavonois kaempferol, quercetin and myricetin. The flavonols are colourless but act as copigments with the anthocyanins to enhance flower colour.
The next step in the pathway leading to the production of the coloured anthocyanins involves dihydroflavonol-4-reductase (DFR) with the production of the leucoanthocyanidins. These flavonoid molecules are unstable under normal physiological conditions and glycosylation at the 3-position, through the action of glycosyltransferases, stabilizes the anthocyanidin molecule thus allowing accumulation of the anthocyanins. In general, the glycosyltransferases transfer the sugar moieties from UDP sugars and show high specificities for the position of glycosylation and relatively low specificities for the acceptor substrates (Seitz and Hinderer, 1988).
The glycosyltransf

REFERENCES:
patent: 5231020 (1993-07-01), Jorgensen et al.
Ralston et al., (1988), "Sequence of Three Bronze Alleles of Maize and Correlation with the Genetic Fine Structure," Genetics 119: 185-187.
Furtek et al., (1988), "Sequence Comparisons of Three Wild-Type Bronze-1 Alleles from Zea mays," Plant Molecular Biology 11: 473-481.
Wise et al., (1990), "Nucleotide Sequence of the Bronze-1 Homologous Gene from Hordeum vulgare," Plant Molecular Biology 14: 277-279.
Chandler et al., (1989), "Two Regulatory Genes of the Maize Anthocyanin Pathway Are Homologous: Isolation of B Utilizing R Genomic Sequences," The Plant Cell 1(12): 1175-1183.
Jonsson et al., (1984), "Properties and Genetic Control of Anthocyanin 5-O-Glucosyltransferase in Flowers of Petnunia hybrida," Planta 160: 341-347.
Furtek, et al (1988) Plant Molecular Biology 11:473-481.
Ralston, et al. (1988) Genetics 119: 183-197.
Wise, et al (1990) Plant Molecular Biology 14: 277-279.

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