EP0680511A1 - Gene acetyl-coa-carboxylase - Google Patents

Gene acetyl-coa-carboxylase

Info

Publication number
EP0680511A1
EP0680511A1 EP94905669A EP94905669A EP0680511A1 EP 0680511 A1 EP0680511 A1 EP 0680511A1 EP 94905669 A EP94905669 A EP 94905669A EP 94905669 A EP94905669 A EP 94905669A EP 0680511 A1 EP0680511 A1 EP 0680511A1
Authority
EP
European Patent Office
Prior art keywords
dna sequence
plants
acetyl
dna
coa carboxylase
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP94905669A
Other languages
German (de)
English (en)
Inventor
Reinhard TÖPFER
Wolfgang Schulte
Jeff Schell
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Max Planck Gesellschaft zur Foerderung der Wissenschaften
Original Assignee
Max Planck Gesellschaft zur Foerderung der Wissenschaften
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Priority claimed from DE4317260A external-priority patent/DE4317260A1/de
Application filed by Max Planck Gesellschaft zur Foerderung der Wissenschaften filed Critical Max Planck Gesellschaft zur Foerderung der Wissenschaften
Publication of EP0680511A1 publication Critical patent/EP0680511A1/fr
Withdrawn legal-status Critical Current

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Classifications

    • 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
    • C12N9/93—Ligases (6)
    • 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
    • C12N15/8247—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 lipid metabolism, e.g. seed oil composition

Definitions

  • the invention relates to a DNA sequence which codes for the acetyl-CoA carboxylase, and the alleles and derivatives of this DNA sequence.
  • acetyl-CoA carboxylase (EC 6.4.1.2) is an important key enzyme in the fatty acid metabolism of prokaryotes and eukaryotes. In a two-step reaction, it catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (AW Alberts and PR Vagelos, The Enzymes (Boyer PD ed), Vol. 6, pp. 37-82, 3rd edition, Academic Press, New York, 1972) according to the following reaction equations:
  • BCCP-COO " + acetyl-CoA transcarboxylase BCCP + malonyl-CoA Acetyl-CoA carboxylase (ACC) has been investigated biochemically, particularly in animal systems and E. coli, and molecular biological studies on a wide variety of organisms have recently been carried out, such as in the rat (F. Lopez-Casillas, DH Bai, X. Luo, IS Kong, MS Hermodson and KH Kim, PNAS 85, pp. 5784-5788 (1988)), the chicken (T. Takai, C. Yokoymama, K. Wada and T. Tanabem J. Biol Soc. 263, pp.
  • the ACC enzyme In bacteria, the ACC enzyme consists of three different polypeptide chains, which consist of three functional units consisting of the biotin carboxylase (BC), the biotin carboxy carrier protein (BCCP) and the carboxyl transferase (CT)
  • BC biotin carboxylase
  • BCCP biotin carboxy carrier protein
  • CT carboxyl transferase
  • the ACC of the rat has a molecular weight of 265 kD (Lopez-Casillas et al, supra), that of the yeast a molecular weight of 251 kD (Al-Feel e_t al, supra) and that of plants varies between 210 and 240 kD (Hellyer et al, supra).
  • Table 1 shows an overview of the homologies of the known ACC enzymes.
  • Table 1 shows the percentages of identical amino acids and the degree of homology in acetyl-CoA carboxylases from chicken, from the rat, from the yeast and from E. coli. It is clearly shown that the ACC enzymes also show a relatively high degree of kinship across the various organisms. Despite the large evolutionary gap between rat and chicken on the one hand and yeast on the other hand there is still about 66% homology across the entire amino acid sequence. If individual areas are selected, homologies of approximately 80% to 100% can be found in some sections (Al-Feel et . Al, supra). The same organizational form of eukaryotic ACCs with regard to the sequence of the domains BC-BCCP-CT is remarkable.
  • EP-A-0 469 810 describes a biotin-containing polypeptide with a molecular weight of 50 kD, which is a subunit of a vegetable acetyl-CoA carboxylase.
  • the 229 bp clone CC 8 in FIG. 8 has no amino acid reading frame which has meaningful homology to one of the known ACC amino acid sequences. This inevitably leads to the conclusion that the antibody used in EP-A-0 469 810 is not specific to ACC or at least one subunit of ACC.
  • This object is achieved with a DNA sequence according to claim 1.
  • the invention relates to a DNA sequence which codes for the acetyl-CoA carboxylase, and the alleles and derivatives of this DNA sequence.
  • the invention further relates to genomic clones which contain a DNA sequence which codes for the acetyl-CoA carboxylase, and the alleles and derivatives of this DNA sequence.
  • the invention also relates to a process for the production of plants, plant parts and plant products, in which a DNA sequence which codes for the acetyl-CoA carboxylase is transmitted by genetic engineering.
  • the invention also relates to the use of this DNA sequence for conferring or transferring herbicide resistance or changing the quality and quantity of vegetable oils and fats.
  • FIG. 1 shows a sequence comparison of the amino acid sequences of biotin-dependent and related enzymes in their BC domain
  • FIG. 2 shows the representation of the DNA or amino acid sequence of the degenerate oligonucleotides 3455 and 3464;
  • 3a shows the DNA sequence and the one derived therefrom
  • Figure 4 shows the restriction maps in the genomic
  • FIG. 5 shows the DNA sequence of the acetyl-CoA carboxylase
  • FIG. 6 shows the functional regions in the DNA sequence from FIG. 5 and the amino acid sequences derived from the DNA sequences in the one-letter code
  • Figure 7 is a schematic representation of the functional
  • FIG. 8 shows a Southern blot hybridization (cross hybridization) of different genomic plant DNA with part of the ACC gene of the genomic clone BnACC8.
  • allelic variants and derivatives of the DNA sequence according to the invention are also covered in the context of the invention, provided that these modified DNA sequences code for acetyl-CoA carboxylase.
  • the allelic variants and derivatives include, for example, deletions, substitutions, insertions, inversions or additions of the DNA sequence according to the invention.
  • the gene for acetyl-CoA carboxylase is present in all plants and can therefore be isolated from them in various ways.
  • the gene can be isolated with the aid of oligonucleotide probes or specific antibodies from genomic plant DNA banks or its cDNA from cDNA banks. Rapeseed (Brassica napus) of the Akela variety has proven to be a particularly suitable plant material.
  • a genome of the rape genome (Brassica napus) of the Akela variety was used as a starting material for the isolation of genomic clones which contain the gene for the ACC, and was set up in a phage.
  • This gene bank was searched for genes for the ACC using a hybridization probe produced by means of PCR (polymerase chain reaction).
  • PCR polymerase chain reaction
  • BnACC8 a genomic clone called BnACC8 was isolated, which contains the complete structural gene (protein coding region (exons and introns)) of the ACC from oilseed rape on a 13.7 kb Xbal fragment. This genomic clone is deposited under the number DSM 7384.
  • genomic clones BnACC3, BnACCIO and BnACCl were isolated, which likewise contain the structural gene of the ACC from rapeseed or at least parts thereof on approximately 20 kb, 15 kb and 15 kb DNA fragments, respectively.
  • the 13.7 kb DNA fragment was subcloned in the form of Xbal / Smal fragments into suitable vectors and sequenced.
  • the amino acid sequences derived from the DNA sequences were compared with the ACC amino acid sequence of the rat from FIG. 2 of the article by F. Lopez-Casillas, supra, by computer analysis. It has been found on the basis of amino acid sequence homologies that the 13.7 kb DNA fragment contains the acetyl-CoA carboxylase gene.
  • an approximately 2 kb DNA fragment of the approximately 20 kb DNA sequence from BnACC3 was sequenced.
  • FIG. 4 shows the restriction maps of the DNA fragments inserted in the genomic clones BnACC3, BnACC8, BnACCIO and BnACCl.
  • BnACC3 and BnACC8 which belong to a class of genes.
  • the areas marked in black indicate areas of DNA that hybridize with the probe used.
  • the DNA fragments are delimited by the interfaces of the cloning vector Lambda FI __ “* TI, which are symbolized by” Y ": Xbal, Sacl, Notl, Sacl and Sall on one side or Sall, Sacl, Notl, Sacl and Xbal on the
  • Y Xbal, Sacl, Notl, Sacl and Sall on one side or Sall, Sacl, Notl, Sacl and Xbal on the sequenced areas of the 13.7 kb DNA fragment from BnACC8 and the approximately 2 kb DNA fragment from BnACC3 were marked by white bars.
  • the complete DNA sequence of the 13.753 kb from the 11.9 kb of the 13.7 kb DNA fragment from BnACC8 and 1904 bp of the approximately 20 kb DNA fragment from BnACC3 is shown in FIG. 5.
  • the DNA sequence at the 5 'end comprises the sequence from BnACC3, starting from the second SalI site and extends at the 3' end with 678 bp beyond the EcoRI site of the BnACC8.
  • the DNA sequence of the 11.9 kb of the 13.7 kb DNA fragment from BnACC ⁇ begins at position 1905 in FIG. 5.
  • the 13.753 kb DNA fragment contains the acetyl-CoA carboxylase structural gene and the promoter, the structural gene already being on the 11.9 kb of the 13.7 kb DNA fragment from BnACC8.
  • FIG. 6 shows the DNA sequence from FIG. 5 with its functional areas. Regulatory elements such as the CAAT box (positions 2283-2286), the TATA box (positions 2416-2419) and a polyadenylation signal (positions 13284-12289) are underlined.
  • the ATG start codon of the ACC is in position 2506 and the associated TGA stop codon in position 13253.
  • the exon / intron boundaries have been highlighted in black.
  • the corresponding amino acid sequences were given for the black highlighted exon regions in the sequence.
  • the exon / intron limits were determined on the basis of the similarity to acetyl-CoA carboxylases from other organisms (rat) (F. Lopez-Casillas, supra), unless these limits have been determined by means of PCR.
  • the first exon of the gene begins at "ATG" as the start codon with an open reading frame.
  • the 5 'non-translated areas are therefore not highlighted in black.
  • the marking of the last exon ends at the corresponding stop codon, so that the 3 'untranslated region is also not marked.
  • BC biotin carboxylase.
  • the DNA sequence according to the invention which codes for the acetyl-CoA carboxylase, the alleles and derivatives of this DNA sequence can be introduced or transferred into plants for the regulation of the fatty acid metabolism (in the form of anti-sense or overexpression) with the aid of genetic engineering methods .
  • Antisense constructions e.g. with sequences from positions 1905 to 3187, 318 ⁇ to ⁇ lO ⁇ and 11039 to 12646 of the DNA sequence according to the invention from FIG. 6 can be used to inhibit the activity of the ACC in a plant. This can be done in particular by checking fragments of the ACC gene by checking fragments of the ACC gene by means of suitable regulatory elements (promoters) in the seed. This can cause a build-up of acetyl-CoA, since this intermediate can no longer flow into the fatty acid metabolism and thus the metabolism e.g. a plant cell influences:
  • a "suicide gene” can thus be produced if an antisense construction leads to the formation of fatty acids in a Cell is omitted. In the fight against plant diseases, a hypersensitive reaction can be triggered in this way.
  • the genes for the synthesis of, for example, polyhydroxybutyrate (PHB) can be stored in particular tissues / organs / cell types of a plant, preferably storage tissues such as seeds ( Endosperm, cotyledon); Root; various types of tubers) can be expressed. If an ACC antisense construction is simultaneously expressed in the same parts of the plant, the unused acetyl-CoA can be used for the synthesis of PHBs.
  • Oligonucleotides can be derived from the DNA sequence according to the invention in order to synthesize a cDNA or pieces of a cDNA. This cDNA or pieces thereof can be used alone or in conjunction with parts of the genomic clone to isolate a complete cDNA. These cDNA or cDNA pieces can also be used for an antisense expression.
  • individual cDNA fragments or the entire cDNA can be used to complement ACC mutants, for example in microorganisms.
  • microorganisms mutants from E. coli fabE; Silbert et. Al. 1976, J. Bacteriol. 126, pages 1351-1354); Harder et al. 1972, PNAS 69, pages 3105-3109 and from yeast (Schweizer et . Al. About i960) under non-permissive conditions functionally complemented by the vegetable ACC and are directly dependent on the vegetable enzyme.
  • yeast yeast
  • the cDNA can also be used to recover larger amounts of the protein or parts of the protein.
  • This manufactured protein can be used for studies on the reaction mechanism and the regulation or to elucidate the three-dimensional structure of the enzyme or parts of the enzyme. The latter point is particularly important for a "protein modeiling", since it allows the adaptation of e.g. Inhibitors allowed in the structure of the protein.
  • the ACC gene sequence, the alleles and derivatives of this sequence are preferably introduced into the plants together with suitable promoters, in particular in recombinant vectors.
  • the DNA sequence according to the invention which codes for the ACC, can be used in particular to achieve herbicide resistance in useful plants, including in particular cereal plants, against certain herbicides.
  • Maize, wheat, barley, rice and rye can be mentioned as preferred plants to be transformed.
  • the genetic engineering introduction of the ACC-DNA sequence, the alleles and derivatives of this sequence can be carried out using conventional transformation techniques.
  • Such techniques include methods such as direct gene transfer, such as microinjection, electroporation, particle gun, viral Vectors and liposome-mediated transfer as well as the transfer of corresponding recombinant Ti plasmids or Ri plasmids and the transformation by plant viruses.
  • the detection of the transformation can be carried out by selection with a suitable herbicide. Furthermore, the detection can be carried out by Southern blots with, for example, intron sequences of the rapeseed ACC DNA as a hybridization probe.
  • the invention thus also relates to plants, plant parts and plant products which have been produced or transformed by one of the above processes.
  • FIG. 1 shows a sequence comparison of the amino acid sequence of biotin-dependent and related enzymes in their BC domain.
  • EACC ACC from E. coli
  • cACC ACC from chicken
  • rPCCof ⁇ subunit of the propionyl-CoA carboxylase from the
  • oligonucleotides were synthesized on an Applied Biosystems DNA synthesizer (Model 380B) and are shown in FIG. 2. Both oligonucleotides are shown in 5 '-3' orientation, so that when comparing with FIG. 1, the amino acid sequence of oligonucleotide 3464 must be read in the opposite direction.
  • oligonucleotides e.g. C or T or A or G in oligonucleotide 3464.
  • I was introduced, which can interact with all nucleotides and is therefore to be regarded as a non-specific base.
  • Avian myeloblostosis virus (AMV) was used to reverse transcriptase for 30 minutes at a temperature of. 37 C performed a cDNA synthesis with the oligonucleotide 3464 as a primer. After inactivity Reverse transcriptase by heating for five minutes at a temperature of 95 C, the PCR reaction with 50 pmol final concentration per primer (3455 and 3464) and four units of Ampli-Ta ⁇ p ⁇ polymerase (Perkin Elmer Cetus) was carried out in the same reaction mixture . The reactions were carried out under the following conditions:
  • Reaction temperatures 3 minutes at a temperature of 92 C for the first denaturation, then 30 temperature cycles with 2 minutes each at a temperature of 92 C for the denaturation, 2 minutes at a temperature of 51 C for annealing the oligonucleotides and 2.5 minutes a temperature of 72 ° C for amplification of the DNA and finally 2.5 minutes at a temperature of 72 ° C to achieve a complete synthesis of the last synthesis products.
  • DNA fragments were amplified by means of PCR reactions after a first-strand cDNA synthesis.
  • the oligonucleotides required for this were synthesized on the basis of a homology comparison inter alia between the ACC from the chicken and from E. coli (FIG. 1). Mathematically, these (degenerate) oligonucleotides should be able to amplify a product of 260 bp length, which codes for 86 amino acids. Amplification products of this magnitude were therefore isolated from the product mixture obtained, cloned in pBluescripr- ⁇ and identified by DNA sequencing.
  • Example 2 Characterization of a genomic clone with a DNA sequence coding for ACC
  • FIG. 4 shows the restriction maps of the genomic clones BnACC3, BnACC ⁇ , BnACCIO and BnACCl.
  • the clone, BnACC ⁇ which belongs to the most frequently represented class, contains a DNA fragment with a size of 13.7 kb. This DNA fragment comprises the complete structural gene of the ACC from rapeseed.
  • the DNA fragment was in the form of Xbal

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Abstract

L'invention concerne une séquence d'ADN qui code l'acétyl-CoA-carboxylase, ainsi que les allèles et les dérivés de cette séquence d'ADN. La séquence du gène acétyl-CoA-carboxylase peut être utilisée pour obtenir, par expression hétérologue, des variétés de plantes, par ex. des plantes céréalières, qui soient résistantes aux herbicides destinés aux graminées, ou bien pour modifier la qualité et la quantité d'huiles et de graisses végétales, par expression homologue ou hétérologue.
EP94905669A 1993-01-22 1994-01-21 Gene acetyl-coa-carboxylase Withdrawn EP0680511A1 (fr)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
DE4301694 1993-01-22
DE4301694 1993-01-22
DE4317260A DE4317260A1 (de) 1993-01-22 1993-05-24 Acetyl-CoA-Carboxylase kodierende DNA-Sequenz
DE4317260 1993-05-24
PCT/EP1994/000150 WO1994017188A2 (fr) 1993-01-22 1994-01-21 Gene acetyl-coa-carboxylase

Publications (1)

Publication Number Publication Date
EP0680511A1 true EP0680511A1 (fr) 1995-11-08

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Application Number Title Priority Date Filing Date
EP94905669A Withdrawn EP0680511A1 (fr) 1993-01-22 1994-01-21 Gene acetyl-coa-carboxylase

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EP (1) EP0680511A1 (fr)
JP (1) JPH08509116A (fr)
CA (1) CA2150678A1 (fr)
WO (1) WO1994017188A2 (fr)

Families Citing this family (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5539092A (en) * 1992-10-02 1996-07-23 Arch Development Corporation Cyanobacterial and plant acetyl-CoA carboxylase
US6069298A (en) * 1993-02-05 2000-05-30 Regents Of The University Of Minnesota Methods and an acetyl CoA carboxylase gene for conferring herbicide tolerance and an alteration in oil content of plants
US6414222B1 (en) 1993-02-05 2002-07-02 Regents Of The University Of Minnesota Gene combinations for herbicide tolerance in corn
US6222099B1 (en) 1993-02-05 2001-04-24 Regents Of The University Of Minnesota Transgenic plants expressing maize acetyl COA carboxylase gene and method of altering oil content
GB9306490D0 (en) * 1993-03-29 1993-05-19 Zeneca Ltd Plant gene specifying acetyl,coenzyme a carboxylase and transformed plants containing same
US6133506A (en) * 1993-09-04 2000-10-17 Max-Planck-Gesellschaft Zur Forerung Der Wissenschaft E.V. Keto-acyl-(ACP) reductase promoter from cuphea lanceolata
WO1995029246A1 (fr) * 1994-04-21 1995-11-02 Zeneca Limited Gene vegetal specifiant l'acetyl-coenzyme a-carboxylase et plantes transformees contenant ce gene
US5925805A (en) * 1994-05-24 1999-07-20 Board Of Trustees Operating Michigan State University Methods of increasing oil content of seeds
US5962767A (en) * 1994-05-24 1999-10-05 Board Of Trustees Operating Michigan State University Structure and expression of an arabidopsis acetyl-coenzyme A carboxylase gene
WO1996032484A2 (fr) * 1995-04-14 1996-10-17 Arch Development Corporation COMPOSITIONS A BASE D'ACETYL-CoA CARBOXYLASE ET PROCEDES D'UTILISATION
DE19737870C2 (de) * 1997-08-29 1999-07-01 Max Planck Gesellschaft Rekombinante DNA-Moleküle und Verfahren zur Steigerung des Ölgehaltes in Pflanzen
US6306636B1 (en) 1997-09-19 2001-10-23 Arch Development Corporation Nucleic acid segments encoding wheat acetyl-CoA carboxylase
CN1154745C (zh) * 1999-11-09 2004-06-23 浙江省农业科学院 利用反义基因调控籽粒油脂含量的方法

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
AU8142191A (en) * 1990-07-30 1992-02-06 Iowa State University Research Foundation Inc. Plant acetyl-coa carboxylase polypeptide and gene
GB9125330D0 (en) * 1991-11-28 1992-01-29 Commw Scient Ind Res Org Novel dna clones and uses thereof
US5539092A (en) * 1992-10-02 1996-07-23 Arch Development Corporation Cyanobacterial and plant acetyl-CoA carboxylase

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO9417188A3 *

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JPH08509116A (ja) 1996-10-01
WO1994017188A2 (fr) 1994-08-04
WO1994017188A3 (fr) 1994-10-13
CA2150678A1 (fr) 1994-08-04

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