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WO1998005760A2 - Proteines pouvant etre induites en cas de privation de phosphate - Google Patents

Proteines pouvant etre induites en cas de privation de phosphate Download PDF

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Publication number
WO1998005760A2
WO1998005760A2 PCT/CA1997/000532 CA9700532W WO9805760A2 WO 1998005760 A2 WO1998005760 A2 WO 1998005760A2 CA 9700532 W CA9700532 W CA 9700532W WO 9805760 A2 WO9805760 A2 WO 9805760A2
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seq
plant
nucleic acid
protein
dna
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PCT/CA1997/000532
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English (en)
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WO1998005760A3 (fr
Inventor
Daniel D. Lefebvre
Mohammad A. Malboobi
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Queen's University At Kingston
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Publication date
Priority claimed from CA002182421A external-priority patent/CA2182421A1/fr
Priority claimed from US08/688,988 external-priority patent/US6096545A/en
Application filed by Queen's University At Kingston filed Critical Queen's University At Kingston
Priority to AU36167/97A priority Critical patent/AU730471B2/en
Priority to EP97932682A priority patent/EP0917564A2/fr
Priority to BR9710909A priority patent/BR9710909A/pt
Publication of WO1998005760A2 publication Critical patent/WO1998005760A2/fr
Publication of WO1998005760A3 publication Critical patent/WO1998005760A3/fr

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
    • C12N9/1205—Phosphotransferases with an alcohol group as acceptor (2.7.1), e.g. protein kinases
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
    • C12N15/8261—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
    • C12N15/8261—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield
    • C12N15/8262—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield involving plant development
    • C12N15/827—Flower development or morphology, e.g. flowering promoting factor [FPF]
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
    • C12N15/8261—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield
    • C12N15/8271—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield for stress resistance, e.g. heavy metal resistance
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
    • C12N15/8261—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield
    • C12N15/8271—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield for stress resistance, e.g. heavy metal resistance
    • C12N15/8273—Phenotypically and genetically modified plants via recombinant DNA technology with agronomic (input) traits, e.g. crop yield for stress resistance, e.g. heavy metal resistance for drought, cold, salt resistance
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2445—Beta-glucosidase (3.2.1.21)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01021—Beta-glucosidase (3.2.1.21)
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A40/00—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production
    • Y02A40/10—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production in agriculture
    • Y02A40/146—Genetically Modified [GMO] plants, e.g. transgenic plants

Definitions

  • this invention provides means for regulating the response of a photosynthetic organism to varying levels of phosphate in its environment as well as a mechanism for modifying the phosphate metabolism of such organisms.
  • This approach to modifying the phosphate pathways of plants has several advantages over traditional plant breeding methods, most importantly, the modifications can be made quickly and specific traits can be modified, even introducing a new trait which is not part of the plant genome.
  • Figure 11 is a comparison of the 3 ' end of the cDNA sequences of Arabidopsis thaliana psrPK (psrl) and B . nigra psrl with the 3 ' end of the DNA sequences of other protein kinases.
  • Figure 25 is the partial DNA sequence of psrlO (SEQ ID NO:24 and SEQ ID NO:25) from Brassica nigra .
  • Figure 26 is the partial DNA sequence of psrll (SEQ ID NO: 26 and SEQ ID NO: 27) from Brassica nigra .
  • Figures 27A-27B show the Southern Blot analysis of Arabidopsis genomic DNA.
  • Figure 28 is a diagram of Arabidopsis thaliana transformation and production of subsequent generations.
  • B . nigra suspension cells were grown in medium containing 1.25 mM P, for 7 days, so that all cells would be in the same metabolic state. The cells were then subcultured into media with various initial concentrations of P x . Growth conditions for the next 7 days were either severe P. deprivation (0 P , mild P 1 deprivation (1.25 mM P.
  • the protein kinases' substrates could be other components of the phosphate-starvation response pathway or enzymes involved in the response itself. These proteins have no apparent N-termmal signal peptide, organellar targeting sequence or membrane spanning regions, which indicates they probably function in the cytoplasm of the cell.
  • DNA or nucleic acids referred to herein as “isolated” are DNA or nucleic acids separated away from the nucleic acids of the genomic DNA or cellular RNA of their source or origin (e.g., as it exists in cells or in a mixture of nucleic acids such as a library) , and may have undergone further processing.
  • isolated DNA or nucleic acids include DNA or nucleic acids obtained by methods described herein, similar methods or other suitable methods, including essentially pure DNA or nucleic acids, DNA or nucleic acids produced by chemical synthesis, by combinations of biological and chemical methods, and recombinant nucleic acids which are isolated.
  • DNA or RNA having 50% homology, preferably 80% homology, or more preferably 90% homology, or which hybridizes under moderately stringent conditions to the DNA of Claim 3.
  • Truncated nucleic acid sequences of the above-described DNA or nucleic acids which consist of 10-20 or more contiguous nucleotides are also provided and can find use as probes and primers.
  • nucleic acids Polypeptides encoded by these nucleic acids are also encompassed by this invention.
  • an isolated nucleic acid encoding a protein having ⁇ - glucosidase activity and an amino acid sequence with at least 80% sequence homology with SEQ ID NO: 5 or 50% homology with SEQ ID NO : 6 is also provided, as is a nucleic acid encoding a protein having phosphate transporter activity and an amino acid sequence with at least 80% sequence homology with SEQ ID NO 17 or 50% homology with SEQ ID NO: 18.
  • Truncated nucleic acid sequences of the above-described DNA or nucleic acids which consist of 10-20 or more contiguous nucleotides are also provided and can find use as probes and primers .
  • High stringency hybridization procedures can (1) employ low ionic strength and high temperature for washing, such as 0.015 M NaCL/0.0015 M sodium citrate, pH 7.0 (O.lx SSC) with 0.1% sodium dodecyl sulfate (SDS) at 50°C; (2) employ during hybridization, 50% (vol/vol) formamide with 5x Denhardt ' s solution (0.1% weight/volume highly purified bovine serum album ⁇ n/0.1% wt/vol F ⁇ coll/0.1% wt/vol polyvmylpyrrolidone) , 50 mM sodium phosphate buffer at pH 6.5 and 5x SSC at 42°C; or (3) employ hybridization with 50% formamide, 5x SSC, 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate , 5x Denhardt ' s solution, sonicated salmon sperm DNA (50 ⁇ g/ml), 0.1% SDS, and 10% dextran sulfate at 42°
  • This invention also provides nucleic acids and polypeptides with structures that have been altered by different means, including but not limited to, alterations using transposons, site-specific and random mutagenesis, and engineered nucleotide substitution, deletion, or addition.
  • the psrPK gene was recognized to encode a novel protein kinase.
  • Other differential hybridization, cloning and sequencing methods are known to those skilled in the art, and can be employed to obtain the protein kinase genes isolated by the inventors, other psr genes, or homologues thereof .
  • a plant transformed with a recombinant nucleic acid of this invention would over- or under-express a psr protein, either in chosen plant parts or throughout the plant, and/or at different times in the life history of the plant. Changes in plant size, relative sizes of different plant parts, time of flowering, level of phytate, starch and oil accumulated in seeds, or other phenotypic characteristics can thus be engineered.
  • Transformation 170 plants / construct/ transformation experiment trans ormation experiments: A, B, ...
  • transformed plant cells are cultured in an appropriate medium, which can contain selective agents such as antibiotics, where selectable markers are used to facilitate identification of transformed plant cells.
  • Selected transformed plant cells can be induced to form callus tissue. Once callus forms, shoot formation can be encouraged by employing the appropriate plant hormones in accordance with known methods and the shoots transferred to rooting medium for regeneration of plants .
  • Sense or antisense nucleic acid according to the invention can be delivered to cells using any of a variety of methods known to persons skilled in the art.
  • the mature, unmodified protein having the amino acid sequence shown as SEQ ID NO : 2 is predicted to have a molecular weight of 39,040 kDa. Prosite searches were used to determine the following characteristics of the PSRPK protein. It contains ser/thr protein kinase active site between amino acid positions 119-131, and an ATP-binding site between positions 9-33. An hydrophobicity plot of the protein does not indicate any long regions of membrane associated protein and an antigenicity plot of the protein indicates several areas that would be appropriate for employment as peptides for antibody production against the protein. These include but are not restricted to the last 150 amino acids at the C-terminus.
  • An antibody of the invention can be physically coupled to any of a number of detectable substances that are known in the art. These include: a radioisotope, a fluorescent molecule, and an enzyme capable of catalyzing a colorimetric reaction. Examples of such an enzyme include alkaline phosphatase and horseradish peroxidase, which are commonly used in laboratory assays.
  • a more modern approach to modifying the characteristics of plants (and other photosynthetic organisms) is to subject plants to mutagenesis by radiation or chemical treatmen . Such exposure randomly generates mutations in the DNA molecules comprising the plant genome which sometimes produces the desired traits.
  • the mutagenized plants are screened for the traits and subsequently bred. While mutagenesis has the advantage of producing variations in plant DNA much faster than natural selection, it is not possible to select and generate preferred traits; the process is random. Further, exposing plants to mutagenic agents can induce additional, undesirable mutations to the plant genome. Some of these may not be immediately apparent and, further, may not be able to be "bred out" of a plant carrying a useful mutation.
  • Photosynthetic organisms have evolved a number of adaptive strategies to cope with growth-limiting amounts of exogenous inorganic phosphate. These strategies include enhancing the availability of endogenous phosphate (Lefebvre et al . , 1990; Sachay et al . , 1991), and using it efficiently in order to maintain essential metabolic pathways (Duff et al . , 1994), as well as, in times of plenty, storing excess phosphate in vacuoles (Lee et al . , 1990; Mimura et al . , 1990; Tu et al . , 1990) so that it can later be used to replenish the cytoplasmic pool as required (Rebeille et al . , 1983).
  • Another embodiment of this invention is the increase in expression of a phosphate transporter protein, such as psr ⁇ or a functional portion thereof in a photosynthetic organism to increase absorption of phosphate from the environment .
  • a phosphate transporter protein such as psr ⁇ or a functional portion thereof in a photosynthetic organism to increase absorption of phosphate from the environment .
  • These proteins can also be used in phytoremediation applications.
  • Pi deficiency can be stimulated with regulatory protein genes which make the plant or other photosynthetic organism absorb and store more Pi because of the inefficiency of use of Pi.
  • photosynthetic organisms can be modified to increase the nutritive value of vegetative or reproductive organs.
  • seed plants such as canola, soybean and corn, store phosphate m the form of phytate (the salt of 1, 2, 3, 4, 5, 6- cyclohexanehexolphosphoric acid) .
  • phytate the salt of 1, 2, 3, 4, 5, 6- cyclohexanehexolphosphoric acid
  • the presence of phytate is a problem where the seed is made into meal and used as feed for animals.
  • Monogastric animals cannot metabolize phytate and utilize its phosphate.
  • phytate binds to essential minerals, such as calcium, manganese and zinc, making them relatively unavailable to the animal.
  • tissue-specific expression sites can include root hairs for increased phosphate uptake, and other tissues where excessive or inadequate expression can be deleterious to cells and can cause cell death. This can be employed in the production of male sterile lines for hybridization purposes, among other applications.
  • Example 2 ⁇ Extraction of total RNA and ⁇ roRN Total RNA from the harvested B. nigra cells of
  • SDS-PAGE denaturing SDS-polyacrylamide gel electrophoresis
  • LKB 2010 Macrophor electrophoresis apparatus Pharmacia Biotech, Inc., Baie d'Urfe, Canada
  • Laemmli Laemmli, 1970
  • Molecular weight standards electrophoresed in parallel were 14 C-labelled ⁇ -lactalbumin, carbonic anhydrase, glyceraldehyde- 3 -phosphate dehydrogenase, chicken egg albumin and bovine serum albumin having molecular weights of 14, 29, 36, 45 and 66 kDa, respectively (Sigma, St.
  • the gels were 0.4 mm thick slabs containing 1% SDS.
  • the acrylamide monomer concentrations were 5% (w/v) for the stacking gel and 10% for the separating gel.
  • the separating gel was 35 cm long, to maximize resolution of protein species. Electrophoresis was performed at 25°C for 5 h at a constant current of 30 mA.
  • FIG. 3 is a summary of the standardized data of the expression differences between polypeptides produced from 10 mM P ⁇ fed, 1.25 mM P,-fed and P ⁇ deprived cells. Based on these analyses, P, deprivation caused the copy number of mRNAs to increase for ten polypeptides, whereas six others decreased. Of translatable RNAs showing altered expression, four species corresponding to proteins with estimated molecular weights of 31.7, 32.3, 52.5, and 64.8 kDa were only detected in the P,-starved treatment.
  • Membranes to which DNA from the isolated clones was bound were first baked for 30 min. at 80 °C, then prehybridized for 5 min. at 65°C in 0.25 M NaH 2 P0 4 (pH 7.2), 7% SDS, 1 mM EDTA. Next, radiolabelled probe was added and hybridization was allowed to proceed for 2 hr . The membranes were then washed twice in 40 mM NaH 2 P0 4 (pH 7.2), 5% SDS, 1 mM EDTA and twice in 40 mM NaH 2 P0 4 (pH 7.2), 1% SDS, 1 mM EDTA, each time for 30-60 min. at 65 °C. Autoradiography was as described above.
  • RNA extracted from each of the minus P.-treated, 1.25 mM P,-fed and 10 mM P x -fed cells were electrophoresed on a 2.2 M formaldehyde/ 1% agarose gel (Sambrook et al . , 1989) and transferred to Nytran Plus membrane (Schleicher & Schuell) according to the manufacturer's protocol.

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Abstract

Cette invention concerne des protéines, notamment des kinases, glucosidases et des agents de transport de phosphate, lesquelles sont exprimées dans des conditions de privation de phosphate. On décrit en outre des acides nucléiques et des constructions d'acides nucléiques codant ces protéines, des cellules contenant les acides nucléiques décrits et des organismes transgéniques de photosynthèse possédant une activité modifiée d'enzyme induite par phosphate.
PCT/CA1997/000532 1996-07-31 1997-07-30 Proteines pouvant etre induites en cas de privation de phosphate WO1998005760A2 (fr)

Priority Applications (3)

Application Number Priority Date Filing Date Title
AU36167/97A AU730471B2 (en) 1996-07-31 1997-07-30 Phosphate starvation-inducible proteins
EP97932682A EP0917564A2 (fr) 1996-07-31 1997-07-30 Proteines pouvant etre induites en cas de privation de phosphate
BR9710909A BR9710909A (pt) 1996-07-31 1997-07-30 Acido desoxirribonucl-ico polipeptideo isolado  cido nucl-ico isolado vetor de expressÆo recombinante celula planta semente cultura de tecido organismo fotossint-tico c-lula procariÄtica descendente m-todo para produzir uma planta anticorpo m-todo para detectar a expressÆo de uma quinase de proteina m-todo para detectar a expressÆo de uma b-glucosidade sequencia de  cidos nucl-icos e m-todo para alterar a tolerancia ao frio ou ao congelamento em uma planta

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
CA002182421A CA2182421A1 (fr) 1996-07-31 1996-07-31 Proteines exprimees dans des conditions de carence en phosphate
CA2,182,421 1996-07-31
US08/688,988 US6096545A (en) 1996-07-31 1996-07-31 Phosphate starvation-inducible proteins
US08/688,988 1996-07-31

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WO1998005760A2 true WO1998005760A2 (fr) 1998-02-12
WO1998005760A3 WO1998005760A3 (fr) 1998-10-08

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CN (1) CN1226925A (fr)
AU (1) AU730471B2 (fr)
BR (1) BR9710909A (fr)
WO (1) WO1998005760A2 (fr)

Cited By (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1998038295A1 (fr) * 1997-02-24 1998-09-03 Performance Plants, Inc. Promoteur activable par une deficience en phosphate
WO2000028012A3 (fr) * 1998-11-10 2000-09-14 Pioneer Hi Bred Int UTILISATION DE β-GLUCOSIDASE POUR AMELIORER LA RESISTANCE AUX MALADIES ET LA RESISTANCE AUX INSECTES DE PLANTES CULTIVEES
WO2003074688A2 (fr) * 2002-03-06 2003-09-12 MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. Polynucleotides codant une beta-glucosidase et utilisations associees
KR100401007B1 (ko) * 2000-08-11 2003-10-08 윤성중 담배의 인산수송자 유전자
WO2006008271A1 (fr) * 2004-07-16 2006-01-26 Cropdesign N.V. Plantes aux caracteristiques de croissance ameliorees et procedes d'obtention correspondants
EP2540832A1 (fr) * 2006-08-02 2013-01-02 CropDesign N.V. Installations dotées de caractéristiques améliorées, transformées avec un petit kinase inductible, et procédé de fabrication de celles-ci
US9055752B2 (en) 2008-11-06 2015-06-16 Intercontinental Great Brands Llc Shelf-stable concentrated dairy liquids and methods of forming thereof
CN105219852A (zh) * 2015-09-25 2016-01-06 南京大学 一种检测鱼腥藻磷代谢相关酶基因表达量引物及应用与方法
US9709551B2 (en) 2013-01-29 2017-07-18 Creative Scientist, Inc. Method for determining the sensitivity of an individual to low dose ionizing radiation
US11490629B2 (en) 2010-09-08 2022-11-08 Koninklijke Douwe Egberts B.V. High solids concentrated dairy liquids

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5413920A (en) * 1992-04-08 1995-05-09 Purdue Research Foundation Method for enhanced production and recovery of phosphate starvation inducible gene products
JP3474882B2 (ja) * 1996-03-25 2003-12-08 王子製紙株式会社 植物のリン酸トランスポーター遺伝子及び該遺伝子を用いた植物の成長を制御する方法
WO1998004701A1 (fr) * 1996-07-29 1998-02-05 Purdue Research Foundation Procedes et compositions pour ameliorer la capacite d'une plante a absorber le phosphate du sol

Cited By (17)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1998038295A1 (fr) * 1997-02-24 1998-09-03 Performance Plants, Inc. Promoteur activable par une deficience en phosphate
US5922564A (en) * 1997-02-24 1999-07-13 Performance Plants, Inc. Phosphate-deficiency inducible promoter
US6175060B1 (en) 1997-02-24 2001-01-16 Performance Plants, Inc. Phosphate-deficiency inducible promoter
WO2000028012A3 (fr) * 1998-11-10 2000-09-14 Pioneer Hi Bred Int UTILISATION DE β-GLUCOSIDASE POUR AMELIORER LA RESISTANCE AUX MALADIES ET LA RESISTANCE AUX INSECTES DE PLANTES CULTIVEES
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WO1998005760A3 (fr) 1998-10-08
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EP0917564A2 (fr) 1999-05-26
AU3616797A (en) 1998-02-25
BR9710909A (pt) 1999-08-17

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