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...
Patent
1995-12-18
1999-01-12
Fox, David T.
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...
435 691, 435101, 4351723, 800250, 800DIG44, 800DIG55, 800DIG56, 536 235, 536 236, A01H 500, C12N 1512, C12N 1529, C12N 1582, C12P 1904
Patent
active
058593330
DESCRIPTION:
BRIEF SUMMARY
FIELD OF THE INVENTION
This invention relates to novel plants having an altered ability to synthesise starch, and to processes for obtaining such novel plants.
Starch is an important end-product of carbon fixation during photosynthesis in leaves and is an important storage product in seeds and fruits. Starch comprises up to 75% of the grain dry weight in cereals. In economic terms, the starch produced by the edible portions of three grain crops, wheat, rice and maize, provide approximately two-thirds of the world's food calculated as calories.
Starch is synthesised in the plastid compartment (the chloroplast in photosynthetic cells or the amyloplast in non-photosynthetic cells). The biochemical pathway of starch biosynthesis in leaves has been well-characterised and is shown in FIG. 1. The abbreviations used are: G-3-P, glyceraldehyde-3-phosphate; DHAP, dihydroxyacetone phosphate; P.sub.i, orthophosphate; PP.sub.i, inorganic pyrophosphate; ADPG/ADPglucose, adenosine diphosphate glucose; ATP, adenosine triphosphate; UDPG/UDPglucose, uridine diphosphate glucose. The reactions are catalysed by the following enzymes: 1) phosphoglycerate kinase/glyceraldehyde-3-phosphate dehydrogenase, 2) triose-phosphate isomerase, 3) aldolase, 4) fructose-1,6-bisphosphatase, 5) hexose phosphate isomerase, 6) phosphoglucomutase, 7) ADP-glucose pyrophosphorylase, 8) starch synthase, 9) UDP-glucose pyrophosphorylase, 10) sucrose phosphate synthase, 11) sucrose phosphatase, 12) orthophosphate/ triose phosphate translocator, 13) inorganic pyrophosphatase.
Knowledge of the pathway in storage tissues was greatly improved following the development of a method for the isolation of intact amyloplasts from wheat endosperm (apRees, 1990) and our recent research with .sup.13 C labelling studies in wheat and maize (Keeling et al, 1988, Plant Physiology, 87: 311-319; Keeling, 1990, ed. C. D. Boyer, J. C. Shannon and R. C. Harrison, pp.63-78, being a presentation at the 4th Annual Penn State Symposium in Plant Physiology, May 1989). FIG. 2 shows the metabolic pathway of starch biosynthesis in maize endosperm. The abbreviations used are the same as in FIG. 1. The reactions are catalysed by the following enzymes: 1) sucrose synthase, 2) UDP-glucose pyrophosphorylase, 3) hexokinase, 4) phosphoglucomutase, 5) hexose-phosphate isomerase, 6) ATP-dependent phosphofructokinase, 7) PP.sub.i -dependent phosphofructokinase, 8) aldolase, 9) triose-phosphate isomerase, 10) hexose-phosphate translocator, 11) ADP-glucose pyrophosphorylase, 12) starch synthase, 13) sucrose phosphate synthase, 14) sucrose phosphatase.
Despite this considerable progress, the first priming molecule(s) responsible for initiating starch synthesis in plants have remained an enigma.
In the animal kingdom, glycogen is deposited rather than starch. It is now well established that glycogen synthesis is initiated on a protein primer which remains covalently attached to the mature macromolecule. Recent work on glycogen deposition has identified a new enzyme: glycogenin or self glucosylating protein (SGP) which acts as a primer. The protein primer serves as the anchor on which the oligosaccharide is constructed and on which glycogen is built (Kennedy et al, 1985, Membranes and Muscle ed. by M. C. Berman et al, IRL Press Oxford/ICSU Press, pp65-84). The linkage between the oligosaccharide and glycogenin involves a novel carbohydrate-protein bond, via the hydroxyl group of tyrosine (Rodriguez and Whelan, 1985, Biochem Biophys Res Commun, 132:829-836). The discovery of glycogenin as a covalent component of the glycogen molecule was followed by the discovery in muscle and other tissues of a glycogen-free form that could be revealed by glucosylation from .sup.14 C-labelled UDPglucose (Rodriguez et al, 1986, Proc 18th Miami Winter Symposium, ICSU Short Reports, 4:96-99). On purification to homogeneity, the protein proved to be autocatalytic. It glucosylates itself and in doing so constructs a maltosaccharide chain on itself that primes glycogen synthesis by glycogen synthase and branching en
REFERENCES:
patent: 5095174 (1992-03-01), Vandeventer et al.
Ardila et al, "Potato Tuber UDP-Glucose: Protein Transglucosylase Catalyzes Its Own Glucosylation", Plant Physiol. 99, (1992) ppl. 1342-1347.
Campbell et al, "The amino acid sequence of rabbit skeletal muscle glycogenin", European Journal of Biochemistry, vol. 185, No. 1 Oct (11) 1989 pp. 119-125.
Quentmeier et al, "Purification of an autocatalytic protein-glycosylating enzyme from cell suspensions of Daucus carota L.", Planta, 171 (1987) 483-488.
FASEB Journal 1992 FASEB Meeting Apr. 5-9, 1992, vol. 6, No. 4, 26 Feb. 1992, p. A1520, Abstract 3382, Gieowar-Singh, D., et al "Purification of self-glucosylating protein from sweet corn."
FASEB Journal 1991 75th Annual Meeting Apr. 21-25, vol. 5, No. 6, Mar. 19, 1991 p. A1547, Abstract No. 6829, Viskupic, et al, "Molecular cloning of a cDNA encoding rabbit skeletal muscle glycogenin."
Rodriguez et al "Peptide characterization and complementary DNA cloning of glycogenin" Invest. Ophthmol. Visual Sci. Annual Meeting Apr. 30-May 5, 1989, vol. 30, 1989 (3 Suppl.) p. 288 Abstract 30.
Smith et al. 1988. Nature 334: 724-726.
Napoli et al. 1990. Plant Cell 2: 279-289.
Snead et al. 1983. Proc. Natl. Acad. Sci. USA 80(23): 7254-7258.
Viskupic et al. 1992. J. Biol. Chem. 267(36): 25759-25763.
Gieowar-Singh Dave
Keeling Peter Lewis
Lomako Joseph
Singletary George William
Whelan William Joseph
Fox David T.
The University of Miami
Zeneca Limited
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