Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Patent
1995-08-15
1999-06-15
Wax, Robert A.
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
536 231, 536 236, 435232, 4352523, 43525233, 435410, 4353201, C07H 2104
Patent
active
059123338
DESCRIPTION:
BRIEF SUMMARY
TECHNICAL FIELD
The present invention relates to a novel DNA which encodes carbonic anhydrase of a monocotyledon.
BACKGROUND ART
Carbonic anhydrase (carbonic dehydratase) is an enzyme widely occurring in animals and plants, which catalyzes the following reaction. preventing evaporation of CO.sub.2 from chloroplasts by converting CO.sub.2 to carbonate ion. One of substrates of ribulose bisphosphate carboxylase (Rubisco) which is an enzyme for carbon dioxide fixation is CO.sub.2. Thus, it is thought that carbonic anhydrase supplies the substrate of Rubisco. Localization of carbonic anhydrase in cells of higher plants varies depending on the type of photosynthesis of the plant. In C.sub.3 plants, carbonic anhydrase activity is found in chloroplasts and in C.sub.4 plants, carbonic anhydrase activity is mainly found in cytoplasm of mesophyll cells.
As mentioned above, carbonic anhydrase catalyzes the reaction by which equilibrium between CO.sub.2 and hydrogen carbonate ion (HCO.sub.3.sup.-) in a solution is maintained. Although this equilibrium is reached under natural conditions, it takes a long time to reach the equilibrium if the enzyme does not participate. Therefore, if this enzyme is introduced by genetic engineering technique into a C.sub.3 plant in which the enzyme is not localized in cytoplasm, it is thought that the reaction to reach the equilibrium between CO.sub.2 and HCO.sub.3.sup.- is promoted and so the substrate of the enzyme carrying out carbon dioxide fixation is efficiently supplied, so that the ability to carry out carbon dioxide fixation of the plant is promoted.
Recently, it was reported that phosphoenol pyruvate carboxylase (PEPC) which is an enzyme catalyzing the first carbon dioxide fixation reaction of C.sub.4 plants was introduced into a C.sub.3 plant by genetic engineering technique (Hudspeth, R. L. et al., (1992), Plant Physiol. 98:485-464; Katsura IZUI et al., (1993), Plant Cell Technology 5: 74-82). The substrate of this enzyme is HCO.sub.3.sup.-. Since carbonic anhydrase does not exist in cytoplasm of C.sub.3 plants, in order that PEPC expressed in the cytoplasm efficiently functions, it is necessary to sufficiently supply HCO.sub.3.sup.-. Thus, if carbonic anhydrase is introduced into the plant to which PEPC has been introduced, it is thought that HCO.sub.3.sup.- consumed by the enzyme reaction of PEPC is supplied to cytoplasm, so that the ability of carbon dioxide fixation of the plant can be further promoted.
Carbonic anhydrase genes of dicotyledons such as spinach (Burnell, J. N. et al., Plant Physiol 92:37-40 (1990); Fawcett, T. W. et al., J. Biol. Chem. 265:5414-5417), pea (Roeske, C. A. et al., Nucleic Acid Res. 18:3413 (1990); Majeau, N. et al., Plant Physiol. 95:264-268 (1991)), Arabidopsis thaliama (Raines, C. A. et al., Plant Mol. Biol. 20:1143-1148 (1992)) and tobacco (Majeau, N. et al., EMBL Nucleotide Sequence Databases, Accession No. M94135, 1992)) have been isolated and sequenced. However, since the carbonic anhydrases of monocotyledons have enzyme properties different from those of dicotyledons, it is expected that greater effects will be obtained by introducing a carbonic anhydrase gene of a monocotyledon to monocotyledons.
As for carbonic anhydrase genes of monocotyledons, maize carbonic anhydrase gene has been partially sequenced (Keith et al., Plant Physiol. 101:329-332 (1993)). However, the sequenced region is only 210 bp. It is thought that this is too short to encode an active carbonic anhydrase and so cannot be used for genetic manipulation of monocotyledons.
DISCLOSURE OF THE INVENTION
Accordingly, the object of the present invention is to provide a gene encoding a carbonic anhydrase of a monocotyledon.
The present inventors intensively studied to succeed in cloning maize carbonic anhydrase cDNA from maize cDNA library using carbonic anhydrase cDNA of spinach as a probe, and sequencing the cloned gene. The present inventors further succeeded in cloning rice carbonic anhydrase cDNA from rice cDNA library using the thus obtained maize carbonic anhyd
REFERENCES:
Hudspeth et al, Plant Physiol., vol. 98, pp. 458-464 (1992).
Burnell et al, Plant Physiol., vol. 92, pp. 37-40 (1990).
Fawcett et al, The Journal of Biological Chemistry, vol. 265, No. 10, pp. 5414-5417 (1990).
Roeske et al, Nucleic Acids Research, vol. 18, No. 11, p. 3413 (1990).
Majeau et al, Plant Physiol., vol. 95, pp. 264-268 (1991).
Raines et al, Plant Molecular Biology, vol. 20, pp. 1143-1148 (1992).
Keith et al, Plant Physiol., vol. 101, pp. 329-332 (1993).
Majeau et al, Plant Physiol., vol. 100, pp. 1077-1078 (1992).
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Burnell et al. "Light Induction and the Effect of Nitrogen Status upon the Activity of Carbonic Anhydrase . . . " Plant Physiol. 94, 384-387, May 1990.
Sugiharto et al. "Glutamine Induces the N-Dependent Accumulation of mRNA Encoding . . . " Plant Physiol. 100, 2066-2070, Jan. 1992.
Relevant parts of the results of sequence search for Seq ID No's 2, 7, and 9, Feb. 1997.
Izui et al, Plant Cell Technology, vol. 5, No. 2, pp. 74-82 (1993).
di Guan et al., Gene, vol. 67, pp. 21-30 (1988).
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Smith et al., Gene, vol. 67, pp. 31-40 (1988). Transcription-Translation System for the Analysis of Proteins in Vitro and in Vivo, vol. 155 (1987).
Studier et al., Methods in Enzymology, vol. 185, pp. 60-89 (1990).
Burnell James Nigel
Suzuki Shoichi
Japan Tobacco Inc.
Nashed Nashaat T.
Wax Robert A.
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