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WO1994011520A2 - Nouvelles plantes et procedes de production - Google Patents

Nouvelles plantes et procedes de production Download PDF

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Publication number
WO1994011520A2
WO1994011520A2 PCT/GB1993/002305 GB9302305W WO9411520A2 WO 1994011520 A2 WO1994011520 A2 WO 1994011520A2 GB 9302305 W GB9302305 W GB 9302305W WO 9411520 A2 WO9411520 A2 WO 9411520A2
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Prior art keywords
plant
starch
gene
target gene
dna construct
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PCT/GB1993/002305
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English (en)
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WO1994011520A3 (fr
Inventor
Peter Lewis Keeling
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Zeneca Limited
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Priority to AU54285/94A priority Critical patent/AU5428594A/en
Publication of WO1994011520A2 publication Critical patent/WO1994011520A2/fr
Publication of WO1994011520A3 publication Critical patent/WO1994011520A3/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)
    • C12N9/1241—Nucleotidyltransferases (2.7.7)
    • 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
    • C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
    • C12N15/8243—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine
    • C12N15/8245—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine involving modified carbohydrate or sugar alcohol metabolism, e.g. starch biosynthesis
    • 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.)
    • C12N9/1048—Glycosyltransferases (2.4)
    • C12N9/1051—Hexosyltransferases (2.4.1)

Definitions

  • This invention relates to novel plants having an altered ability to produce starch, including an improved ability to produce structurally-altered starch or starch of altered quality.
  • the invention further relates to processes for obtaining such plants.
  • Agriculture uses many crop plants for the production of food for human or animal consumption, for commercial processes yielding products for human consumption, for the development of industrial products and for other purposes.
  • the improvement of crop plant species involves the introduction of desired traits by genetic crosses.
  • These breeding techniques are highly successful, and seed producers sell the resulting seed to the farmer. The farmer plants this seed and harvests the crop, be it the whole plant, its seed or its fruit. The crop is then used for the various applications mentioned above.
  • Starch is an important end-product of carbon fixation during photosynthesis in leaves and is an important storage product in seeds and fruits.
  • 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 amylose and amylopectin
  • This starch is used to produce a wide range of food products (for human and animal consumption) and industrial products (such as glue).
  • Several crop varieties are known which produce different types of starch.
  • the type or quality of starch makes it suitable for certain purposes, including particular methods of processing or particular end-uses.
  • US Patent Serial Numbers 4789557, 4790997, 4774328, 4770710, 4798735, 4767849, 4801470, 4789738, 4792458 and 5009911 describe naturally-occurring maize mutants producing starches of differing fine structure suitable for use in various food products. These mutants include the dull, waxy, amylose extender, shrunken, sugary and floury mutants. Although known mutants produce altered starch, some of these lines are not suitable for crop breeding and/or for the farmers' purposes. For example, they often give relatively poor yields.
  • Improved crops may be produced by genetic manipulation of plants known to possess other favourable characteristics.
  • By manipulating the expression of one or more starch-synthesising enzyme genes it is possible to alter the amount and/or type of starch produced in a plant.
  • One or more enzyme gene constructs which may be of plant, fungal, bacterial or animal origin, are incorporated into the plant genome by sexual crossing or by transformation.
  • the enzyme gene may be an additional copy of the wild-type gene or may encode a modified or allelic or alternative enzyme with improved properties. Incorporation of the enzyme gene construct(s) may have varying effects depending on the amount and type of enzyme gene(s) introduced (in a sense or antisense orientation).
  • Such chemically-inducible promoter sequences may be used in "gene switches” to regulate transcription of an associated DNA sequence (or “target gene”) in plants or plant tissue.
  • the gene switch may be a positive switch, where the inducible promoter directly controls the target gene. In the presence of the chemical inducer, the target gene is switched on and the encoded protein is expressed.
  • the inducible GST 11-27 promoter can be operatively linked to one or more target genes to give a chemically switchable construct: expression of the target gene(s) is controlled by application of an effective exogenous inducer.
  • the gene switch construct may be inserted into a plant by transformation.
  • the inducible GST 11-27 promoter is functional in both monocotyledons and dicotyledons, and in a variety of tissues including roots, leaves, stems and reproductive tissues.
  • Effective inducers for use with the GST 11-27 promoter include N,N-diallyl-2,2-dichloroacetamide (common name: dichloramid) ; benzyl-2-chloro-4-(trifluoromethyl) -5-thiazole-carboxylate (common name: flurazole); naphthalene-1,8-dicarboxylic anhydride; 2-dichloromethyl-2-methyl-l,3-dioxolane and several others as described in International patent application publication numbers O90/08826 and WO93/01294. The contents of the said applications are incorporated herein by reference.
  • the gene switch may be a negative switch, where the inducible promoter indirectly controls the target gene via a repressor/operator system. In the presence of the chemical inducer, the target gene is switched off and the encoded protein is not expressed.
  • the switch comprises a chemically-inducible promoter (A) driving expression of a repressor gene encoding a repressor protein, and a promoter (B) containing an operator sequence and driving expression of a target gene.
  • A chemically-inducible promoter
  • B promoter
  • the operator region may be introduced into promoter(B) by biotechnological techniques). If present, the repressor protein binds to the operator sequence, preventing expression of the target gene.
  • promoter (A) In the absence of inducer, promoter (A) is not active and the repressor protein is not expressed: hence the target gene is expressed, in the presence of the chemical inducer, the repressor protein prevents expression of the target gene.
  • Promoter (A) may be GST 11-27 or any other chemically-inducible promoter sequence.
  • the repressor gene/operator sequences may be taken from the E coli lac operon.
  • a method of producing a plant with switchable starch-synthesising ability comprising stably incorporating into the genome of a recipient plant at least one target gene encoding an enzyme involved in a starch or glycogen biosynthetic pathway and under the control of a gene switch.
  • a plant with switchable starch-synthesising ability may have switchable starch yield, and/or (preferably) switchable starch quality.
  • Crops with switchable starch yield have a chemically regulatable ability to synthesise starch in differing amounts and/or at differing rates and/or at differing temperature optima.
  • Expression of the target gene(s) effects a change in the activities and/or natural ratios of the enzymes or their isoforms which results in the production of differing quantities of starch.
  • Crops with switchable starch quality have a chemically regulatable ability to synthesise starch with an altered fine structure.
  • Expression of the target gene(s) (inserted in a sense and/or an anti- sense orientation) effects a change in the activites and/or natural ratios of the enzymes or their isoforms which results in the production of differing qualities of starch.
  • the fine branching structure of starch is determined by the overall activities of the various isoforms of the starch synthases and branching enzymes being expressed during starch deposition in the developing endosperm.
  • starch synthetase and branching enzyme and/or the source of the enzymes alters the fine-branching structure of the starch.
  • the invention further provides a DNA construct which comprises at least one target gene encoding an enzyme involved in a starch or glycogen biosyntheti-c pathway and under the control of a gene switch.
  • the invention also provides plants transformed with said DNA construct, the seeds and progeny of such plants, and hybrids whose pedigree includes such plants.
  • the target gene encodes one or more of the following enzymes: soluble starch synthase (SSS) (E.C. 2.4.1.21); branching enzyme (BE) (E.C. 2.4.1.18); glycogen synthase (GS) of bacterial origin (E.C. 2.4.1.21) or animal origin (E.C. 2.4.1.11); ADP-glucose pyrophosphoryiase; glycogenin, amylogenin or self glucosylating protein (SGP) .
  • SSS soluble starch synthase
  • BE branching enzyme
  • GGS glycogen synthase
  • GS glycogen synthase
  • E.C. 2.4.1.21 bacterial origin
  • animal origin E.C. 2.4.1.11
  • ADP-glucose pyrophosphoryiase glycogenin, amylogenin or self glucosylating protein (SGP) .
  • the target gene is obtainable from any suitable bacterial, fungal (including yeast), plant or animal source.
  • the target gene may be derived from cDNA or genomic DNA (gDNA) encoding a starch or glycogen synthetic enzyme, or it may be synthesised a_b initio using standard techniques.
  • the target gene encodes at least part of an enzyme involved in a starch or glycogen biosynthetic pathway.
  • the target gene may encode the complete enzyme in the sense orientation so that the transcription product (mRNA) can be translated into the active enzyme.
  • the target gene may encode a portion of the enzyme in the sense orientation or may encode some or all of the enzyme in the antisense orientation so that the transcribed mRNA inhibits expression of the enzyme. It is possible to insert more than one copy of the target gene into the recipient plant genome.
  • At least one of the target genes may encode a modified allelic form of the enzyme having altered characteristics (such as increased or decreased activity, or differing interactions with other enzymes) .
  • the enzyme encoded by the target gene When the enzyme encoded by the target gene must be expressed within the plastid compartment, the protein must be transported into the amyloplast (or chloroplast) by means of a transit peptide.
  • a suitable transit peptide-encoding sequence must therefore precede the target gene sequence.
  • the gene switch may be a positive or a negative switch which is responsive to a chemical inducer.
  • the gene switch includes a gene promoter which is inducible by application of an exogenous chemical inducer, and which is operatively linked (directly or indirectly) to control expression of the target gene within a plant genome. It gives the ability to switch the target gene(s) on or off as desired. Using a positive gene switch
  • inducible promoter alone presence of a chemical inducer switches the target gene on and the crop contains starch of altered fine structure.
  • the target gene In the absence of a chemical inducer, the target gene is inactive and starch has its "normal” structure.
  • a negative gene switch inducible promoter with repressor/operator system
  • the target gene is switched on in the absence of chemical inducer, giving starch of altered fine structure.
  • the target gene is switched off in the presence of chemical inducer giving starch of "normal" structure.
  • the inducible promoter may be the gene promoter for the 27 kD subunit of the glutathione-S-transferase, isoform II, enzyme (GST 11-27), although it is clear that additional chemically induced promoters may be used. Some of these may be of plant origin, others may be of fungal (including yeast) origin.
  • a genomic DNA sequence encoding the GST 11-27 gene promoter (having the nucleotide sequence shown in Figure 5) was deposited on 14 June 1991 in the National Collections of Industrial and Marine
  • NCIMB Bacteria
  • NCIMB Bacteria
  • 23 St Machar Drive Aberdeen, AB2 1RY, Scotland, UK
  • plasmid pGIE7 contained within Escherichia coli
  • strain XLI-Blue with the accession number NCIMB 40426.
  • a cDNA sequence (having the nucleotide sequence shown in Figure 6) encoding this GST 11-27 subunit was deposited on 19 April 1991 in NCIMB as plasmid pIJ21 contained within Escherichia coli, strain XLI-Blue with the accession number NCIMB 40413.
  • the plasmid p35SlacI containing DNA encoding a repressor/operator system as described in International patent application publication number WO90/08829 was deposited in an E.coli , strain TG-2, host with the National Collection of Industrial and Marine Bacteria Limited, Aberdeen, United Kingdom, on 12th December 1988, under the Accession Number NCIB 40092.
  • the plasmid pPSl a derivative of pADl ⁇ , was also deposited under the terms of the Budapest Treaty, in an Escherichia coli, strain DH5 ⁇ , host, with NCIMB on 21 December 1988, under the accession Number 40097.
  • the target gene(s) are incorporated into the genome of the recipient plant by sexual crossing or by transformation.
  • the method employed for transformation of the plant cells is not especially germane to this invention and any method suitable for the target plant may be employed. Numerous transformation procedures are known from the literature such as agroinfection using Agrobacterium tumefaciens or its Ti plasmid, electroporation, microinjection of plant cells and protoplasts, microprojectile transformation and pollen tube transformation, to mention but a few. Reference may be made to the literature for full details of the known methods.
  • the transformed cells may then be regenerated into whole transgenic plants in which the new nuclear material is stably incorporated into the genome. Both transformed monocot and dicot plants may be obtained in this way, although the latter are usually more easy to regenerate.
  • the above method is generally applicable to all plants producing or storing starch.
  • the recipient plant may be: a cereal such as maize (corn), wheat, rice, sorghum or barley; a fruit-producing species such as banana, apple, tomato or pear; a root crop such as cassava, potato, yam or turnip; an oilseed crop such as rapeseed, sunflower, oil palm, coconut, linseed or groundnut; a meal crop such as soya, bean or pea; or any other suitable species.
  • the recipient plant is of the family Gramineae and most preferably of the species Zea mays.
  • the method according to the invention may be used to produce a plant having a chemically regulatable ability to synthesise starch with an altered fine structure.
  • the plant has switchable starch quality: the type of starch it produces is responsive to a chemical inducer and so can be externally controlled. It is thus possible to generate crops at will which produce starch better adapted or targetted to the crops' end-use (such as starch for varying food products, with improved processing properties, with improved digestibility, with improved seed production characteristics, etc) .
  • the crops grown by the farmer will need the target enzyme genes switched on to give altered starch structure in the seed produced.
  • the farmer benefits from improved starch quality ("improved" with respect to its intended end-use).
  • improved starch quality is no disadvantage to the farmer as he will not be re-growing the seed and the improved starch quality compensates for any reduced yield.
  • the crops grown by seed producers for seed production will need the target enzyme genes switched off as the "improved quality" starch is not required. Instead, the normal type and amount of starch is required for optimal germination: the seed company merely needs as many normal seeds as possible to maximise production.
  • the seed companies can then supply the "normal" seed to farmers which germinates well to give a good stand.
  • the target enzyme gene(s) may be switched on by the farmer.
  • a preferred embodiment is to use a negative gene switch (inducible promoter with repressor/operator system), so that presence of chemical inducer is needed to switch the enzyme genes off. Hence the farmer does not need to spray his crop with chemicals.
  • the main advantage of the switchable quality crops described above is that plant growth and vigour is guaranteed in the seed production fields and in the farmers' fields, while allowing the farmer to produce seed with altered starch fine structure/improved starch quality at the appropriate time using the same crop variety.
  • Another example of a specific application of the invention is the production of switchable or inducible sweetcorn. This gives the beneficial ability to produce a different type of corn as desired.
  • the shrunken2 or the brittle2 sweetcorn mutant carries a mutation in the ADPG pyrophosphoryiase gene such that sucrose content is the grain increases with a corresponding decrease in starch content.
  • Expression of the normal ADPG pyrophosphoryiase gene within a sweetcorn line allows production of normal starch. If sweetcorn plants are transformed with a normal ADPG pyrophosphoryiase gene under the control of a positive or negative gene switch, the crop grower, has the ability to switch between production of normal starch or sweetcorn by switching the normal ADPG pyrophosphoryiase gene on or off as desired. With a positive gene switch, sweetcorn is produced in the absence of inducer. With a negative gene switch, sweetcorn is produced in the presence of inducer.
  • normal ADPG pyrophosphoryiase gene in a normal corn line would produce sweetcorn. If normal corn plants are transformed with a partial sense or an antisense ADPG pyrophosphoryiase gene construct under the control of a positive or negative gene switch, the crop grower has the ability to switch between production of normal starch or sweetcorn by switching the target gene on or off as desired.
  • sweetcorn With a positive gene switch, sweetcorn is produced in the presence of inducer. With a negative gene switch, sweetcorn is produced in the absence of inducer.
  • Other sweetcorns existing in nature carry mutations in other starch enzyme genes which disrupt starch synthesis and cause the "sweetcorn" phenotype.
  • the sugary sweetcorn mutant carries a mutation in the soluble starch synthase gene
  • the brittlel sweetcorn mutant (Sullivan et al, 1991, Plant Cell, 3(12):1337-1348; Sullivan et al, 1990, J Cell Biochem Suppl, 0 (14 part E):358) may carry a mutation in the amylogenin gene.
  • switchable or inducible sweetcorn may be produced as hereinbefore described with reference to the ADPG pyrophosphoryiase gene using suitable transformation constructs including other target genes.
  • a corn plant comprising a genome lacking an enzyme active in the biosynthesis of starch such that, in its unaltered state, said plant produces seed of the sweetcorn phenotype, said genome further comprising a gene construct, stably incorporated therein by transformation, including a copy of the gene which the unaltered genome lacks, said copy being under the control of a gene switch.
  • the invention also provides seed corn of the genotype described in the preceding paragraph which, when grown in the presence of the inducer of the gene switch, produces corn plants and seed of normal phenotype and which produces seed of the sweetcorn phenotype in the absence of the inducer.
  • the method according to the invention may also be used to produce crops with switchable starch yield; that is, with a chemically regulatable capacity to produce an increased/decreased amount of starch and/or to produce starch at a faster/slower rate and/or at a higher/lower temperature optimum.
  • a crop variety may be produced which is adapted to the growth temperature of a particular environment (including particular sites or geographical regions) by having an improved capacity to produce starch at elevated or lowered temperature. If the enzymes genes controlling this capacity may be switched on or off by external control (a chemical inducer), this crop variety may be adapted to more than one temperature regime.
  • oilseed crops may be transformed with enzyme gene(s) involved in oil production under the control of a gene switch.
  • Figure 1 shows the nucleotide sequence for E coli glycogen synthase.
  • Figure 2 shows the cDNA sequence of wheat leaf ADP-glucose pyrophosphoryiase (clone WL.AGA.l).
  • Figure 3 shows the cDNA sequence of wheat leaf ADP-glucose pyrophosphoryiase (clone WE.AGA.3).
  • Figure 4 shows the cDNA sequence of wheat endosperm ADP-glucose pyrophosphoryiase (clone WE.AGA.7) .
  • Figure 5 shows the nucleotide sequence of the GST 11-27 gene promoter.
  • Figure 6 shows the nucleotide sequence of cDNA encoding GST 11-27.
  • Figure 7 shows the construct pZM/RMS-3.
  • Figure 8 gives an overview of the method of vector construction.
  • Figure 9 is a graph showing GUS activity in endosperm.
  • the construct pZM/RMS-3 (shown in Figure 7) is a stable transformation vector for Zea mays made using standard techniques.
  • the abbreviations used in Figure 7 are as follows: GST (GST 11-27 promoter); GUS ( ⁇ -glucuronidase reporter gene); NOS (nopaline synthase terminator); 35S (Cauliflower mosaic virus 35S promoter); II (maize alcohol dehydrogenase intron 1); BAR (phosphinothricin acyl transferase ) ; TERM (Cauliflower mosaic virus 35S terminator); AMP (prokaryotic ampicillin resistance ) .
  • pZM/RMS-3 was constructed using approximately 3.8 Kb of the GST 11-27 promoter isolated from plasmid pGIE7 (NCIMB 40426). Nde I was used to cut the GST 11-27 promoter at the ATG and 4 Kb ' upstream. This fragment was cut with EcoRI, blunted and cloned into the Smal site of pTAK (a Binl9 based promoterless GUS construct) to give pGSTTAK. The GST-GUS-nos cassette from pGSTTAK was then cloned into a pUC derived vector containing the Bar selectable cassette giving pZM/RMS-3.
  • Figure 8 gives an overview of the method of vector construction.
  • the construct comprises the ⁇ -glucuronidase gene (GUS) under the control of the inducible GST 11-27 promoter.
  • GUS ⁇ -glucuronidase gene
  • the GUS gene was used instead of a starch or glycogen biosynthetic enzyme gene because it is a suitable reporter gene for monitoring gene expression.
  • the construct pZM/RMS-3 was transformed into maize plants using the particle bombardment procedure (Gordon-Kamm et al, 1990, Plant Cell, 2:603-618) .
  • FIG. 9 shows the results for individual kernels which were untreated (U) or treated with 10 ml of 20g/l safener by spraying (S) or root drench (RD). GUS gene expression was determined 48 hours after safener treatment. No GUS expression was observed in endosperm extracts prepared from untreated kernels. Safener spray treatment at 16 dap caused a significant elevation of GUS activity in endosperm. Similarly, spray application and root application of safener at 22 dap caused elevated levels of GUS expression in endosperm. A proportion of the treated kernels show no GUS expression; these represent the azygous progeny from the heterozygous self pollination.
  • RNA transcripts were significantly elevated in induced endosperm and induced embryo (at 14 dap and 24 dap) .
  • Plant transformation vectors for use in the method of the invention may be constructed using standard techniques.
  • the GUS reporter gene used in construct pZM/RMS-3 (Example 1) may be replaced with the required starch or glycogen biosynthetic enzyme sequence.
  • Figure 1 shows the nucleotide sequence for the E coli glgA gene encoding glycogen synthase as retrieved from the GenBank/EMBL (SWISS-PROT) database, accession number J02616 (]Kumar et al, 1986, J Biol Chem, 261:16256-16259).
  • E coli glycogen biosynthetic enzyme structural genes were also cloned by Okita et al (1981, J Biol Chem, 256(13) :6944-6952) .
  • the glycogen synthase glgA structural gene was cloned from Salmonella typhimurium LT2 by Leung et al (1987, J Bacteriol, 169(9) :4349-4354) .
  • the sequences of glycogen synthase from rabbit skeletal muscle (Zhang et al, 1989, FASEB J, 3:2532-2536) and human muscle (Browner et al, 1989, Proc Natl Acad Sci, 86:1443-1447) are also known.
  • the most favoured sources of the glycogen synthase gene for use in this invention are bacterial rather than animal sources because: (1) the bacterial glycogen synthase and plant soluble starch synthase both use ADPG, whereas the animal GS enzyme uses UDPG; (2) the bacterial GS and plant SSS enzymes do not have any phosphorylation sites for activation, whereas the animal enzyme does; and, (3) the animal GS enzyme requires glucose-6-phosphate as a co-factor and is allosterically activated, whereas the plant SSS and bacterial GS enzymes are not.
  • the bacterial and animal GS sequences are not homologous.
  • the structural genes for the bacterial GS are mapped to pOPl2 in E coli and glycogen synthase maps to glgA.
  • Nucleotide sequencing further refined the position of glgA.
  • the translation start point of glgA is known to be immediately following glgC and the nucleotide sequence determined.
  • the NH- sequence was known so that the actual start of the glgA gene was unambiguously determined as well as confirming the direction of transcription.
  • the deduced amino acid sequence shows complete homology with the known NH- sequence and with the known amino acid sequence. Different bacterial enzymes show 90% homology. There is complete agreement between the reported and deduced amino acid sequences for the enzyme. Cells transformed with the gene produce a polypeptide that has sequence homology with the known amino acid sequences.
  • E coli glycogen synthase ( Figure 1) is not a large protein: the structural gene is 1431 base pairs in length, specifying a protein of 477 amino acids with an estimated molecular weight of 49,000. It is known that problems of codon usage can occur with bacterial genes inserted into plant genomes but this is generally not so great with E coli genes as with those from other bacteria such as those from Bacillus. Glycogen synthase from E coli has a codon usage profile much in common with maize genes but it is preferred to alter, by known procedures, the sequence at the translation start point to be more compatible with a plant consensus sequence : glgA G A T A A T G C A G cons A A C A A T G G C T
  • the GS gene construct requires the presence of an amyloplast transit peptide to ensure its correct localisation in the amyloplast. It is believed that chloroplast transit peptides have similar sequences (Heijne et al describe a database of chloroplast transit peptides in 1991, Plant Mol ⁇ Biol Reporter, 9(2 ) :104-126 ) . Other potential transit peptides are those of ADPG pyrophosphoryiase (1991, Plant Mol Biol Reporter, 9:104-126), small subunit RUBISCO, acetolactate synthase, glyceraldehyde-3P-dehydrogenase and nitrite reductase.
  • the consensus sequence of the transit peptide of small subunit RUBISCO from many genotypes has the sequence: MASSMLSSAAVATRTNPAQASMVAPFTGLKSAAFPVSRKQNLDITSIASNGGRVQC and the corn small subunit RUBISCO has the sequence: MAPTVMMASSATATRTNPAQASAVAPFQGLKSTASLPVARRSSRSLGNVA NGGRIRC.
  • the transit peptide of leaf starch synthase from corn has the sequence:
  • the transit peptide of leaf glyceraldehyde-3P- dehydrogenase from corn has the sequence:
  • the putative transit peptide from ADPG pyrophosphoryiase from wheat has the sequence: RASPPSESRAPLRAPQRSATRQHQARQGPRRMC.
  • the genes glc3 and ghal of cerevisiae are allelic and encode the glycogen branching enzyme (Rowen et al, 1992, Mol Cell Biol, 12(1) :22-29) .
  • Matsumomoto et al investigated glycogen branching enzyme from Neurospora crassa (1990, J Biochem, 107:118-122).
  • GenBank/EMBL database also contains sequences for the E coli glgB gene encoding branching enzyme.
  • Branching enzyme [1,4- ⁇ -D-glucan: 1,4- ⁇ -D-glucan 6- ⁇ -D-(1,4- ⁇ -D-glucano) transferase (E.C. 2.4.1.18)] converts amylose to amylopectin, (a segment of a 1,4- ⁇ -D-glucan chain is transferred to a primary hydroxyl group in a similar glucan chain) sometimes called Q-enzyme. Like soluble starch synthase, this reaction also has temperature-dependent properties in plants, presumably because of the same molecular mechanisms of helix-to-chain transitions. It is reasonable to believe that the bacterial BE enzyme will behave similarly.
  • Bacterial branching enzyme genes may be used in this invention, although plant sequences can also be used (rice endosperm: Nakamura et al, 1992, Physiologia Plantarum, 84:329-335 and Nakamura and Yamanouchi, 1992, Plant Physiol, 99:1265-1266; pea: Smith, 1988, Planta, 175:270-279 and Bhattacharyya et al, 1989, J Cell Bioche , Suppl 13D:331; maize endosperm: Singh and Preiss, 1985, Plant Physiology, 79:34-40; Vos-Scherperkeuter et al, 1989, Plant Physiology, 90:75-84; potato: Kossmann et al, 1991, Mol Gen Genet, 230(1-2):39-44; cassava: Salehuzzaman and Visser, 1992, Plant Mol Biol, 20:809-819).
  • Thre fragments from this 86kD BEII protein from B73 maize are shown below:
  • the BE gene construct may require the presence of an amyloplast transit peptide to ensure its correct localisation in the amyloplast, as discussed previously for the glycogen synthase gene.
  • the following segments of plant starch synthase (and E coli glycogen synthase) sequences include the sequence KTGGL which is known to be the ADPG binding site: Pea GEKPPPLAGTNVMNIILVSAECAPWSKTGGLGDVAGSLPKAL Maize ASAGMNWFVGAEMAPWSKTGGLGDVLGGLP Barley ATGSGMNLVFVGAEMAPWSKTGGLGDVLGGLP Potato GKGMNLIFVGTEVGPESKTGGLGDVLGGLP (E coli) MQVLHVCSEMFPLLKTGGLADVIGALP
  • GenBank/EMBL database also contains sequences for the E coli glgC gene encoding ADP-glucose pyrophosphoryiase.
  • FIG. 1 shows the cDNA sequence of wheat leaf ADP-glucose pyrophosphoryiase (clone WL.AGA.l).
  • Figure 3 shows the cDNA sequence of wheat leaf ADP-glucose pyrophosphoryiase (clone WE.AGA.3).
  • Figure 4 shows the cDNA sequence of wheat endosperm ADP-glucose pyrophosphoryiase (clone WE.AGA.7).
  • glycoprotein primer may be a universal feature for the synthesis of polysaccharides such as starch, glycogen, cellulose etc.
  • the priming molecules may be self-glucosylating proteins (SGP), for example glycogenin which acts as a primer for glycogen synthesis in animals or amylogenin which acts as a primer for starch synthesis in plants (Lomako et al, 1988, FASEB J, 2:3097-3103 and 1990, FEBS Lett, 268:8-12 and 1991, FEBS Lett, 279:223-228; Cao et al, 1993, J Biol Chem, 268(20):14687-14693; International patent application number GB93/01821).
  • SGP self-glucosylating proteins
  • the glycogenin protein from rabbit skeletal muscle has been sequenced by Campbell and Cohen (1989, Eur J Biochem, 185:119-125), and a glycogenin cDNA has also been identified (Viskupic et al, 1991, FASEB J, 5(6):A1547 and 1992, J Biol Chem, 267(36) : 25759-25763 ) .
  • the partial amino acid sequencing of peptide fragments of amylogenin from B73 maize was carried out by Gieowar-Singh, Lamoko and Whelan (1992, FASEB J, 6(4) :A1520 and A3382); the amino acid sequences of nine purified tryptic peptides (labelled T1-T9) are shown below.

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Abstract

Un procédé de production d'une plante présentant une aptitude de synthèse d'amidon modifiable consiste à incorporer de manière stable, dans le génome d'une plante réceptrice, au moins un gène cible codant une enzyme impliquée dans une voie biosynthétique d'amidon ou de glycogène, et soumise au contrôle d'une commutation génique. Une plante présentant une aptitude de synthèse d'amidon modifiable peut également présenter un rendement d'amidon modifiable et/ou une qualité d'amidon modifiable et/ou une qualité d'amidon modifiable. Les enzymes biosynthétiques d'amidon ou de glycogène comprennent la synthase d'amidon soluble, l'enzyme de ramification, la glycogène-synthase, l'ADP-glucose pyrophosphorylase, la protéine à auto-glucosylation, la glycogénine et l'amylogénine. Des structures d'ADN utilisées avec ce procédé sont également décrites, ainsi que des plantes transformées au moyen desdites structures, les graines et les descendants de ces plantes, et des hybrides dont l'ascendance comprend ces plantes.
PCT/GB1993/002305 1992-11-09 1993-11-09 Nouvelles plantes et procedes de production WO1994011520A2 (fr)

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WO1997022703A3 (fr) * 1995-12-20 1997-07-24 Du Pont Nouveaux amidons obtenus par modification de l'expression de genes d'enzymes biosynthetiques d'amidon
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