Abstract
A full-length cDNA encoding a subunit of phosphoenolpyruvate carboxylase (PEPC) was isolated from a developing seed expression library of the C3 plant Glycine max. The corresponding mRNA is present at similar levels in leaf, stem, root and developing seed. Two potential start codons exist, and the activity of protein initiated from the first such codon could be subject to regulation by protein kinase. Sequence comparison shows a similar upstream start codon in the case of the Ppc2 gene from Mesembryanthemum crystallinum, previously assumed to lack the sequences necessary for phosphorylation. The soybean encoded protein tends to resemble other ‘C3-type’ PEPC proteins more closely than those implicated in C4 or crassulacean acid metabolism.
References
Ashworth JM, Kornberg HL: The anaplerotic fixation of carbon dioxide by Escherichia coli. Proc Roy Soc Ser B 165: 179–188 (1966).
Cretin C, Keryer E, Tagu D, Lepiniec L, Vidal J, Gadal P: Complete cDNA sequence of sorghum phosphoenolpyruvate carboxylase involved in C4 photosynthesis. Nucl Acids Res 18: 658 (1990).
Cretin C, Santi S, Keryer E, Lepiniec L, Tagu D, Vidal J, Gadal P: The phosphoenolpyruvate carboxylase gene family of Sorghum: promoter structures, amino acid sequences and expression of genes. Gene 99: 87–94 (1991).
Cushman JC, Bohnert HJ: Nucleotide sequence of the ppc2 gene encoding a housekeeping isoform of phosphoenolpyruvate carboxylase from Mesembryanthemum crystallinum. Nucl Acids Res 17: 6743–6744 (1989).
Davies DD: The central role of phosphoenolpyruvate in plant metabolism. Annu Rev Plant Physiol 30: 131–158 (1979).
Hudspeth RL, Grula JW: Structure and expression of the maize gene encoding the phosphoenolpyruvate carboxylase isozyme involved in C4 photosynthesis. Plant Mol Biol 12: 579–589 (1989).
Jiao J-a, Chollet R: Light/dark regulation of maize leaf phosphoenolpyruvate carboxylase by in vivo phosphorylation. Arch Biochem Biophys 261: 409–417 (1988).
Jiao J-a, Chollet R: Regulatory phosphorylation of serine-15 in maize phosphoenolpyruvate carboxylase by a C4-leaf protein-serine kinase. Arch Biochem Biophys 283: 300–305 (1990).
Koizumi N, Sato F, Terano Y, Yamada Y: Sequence analysis of cDNA encoding phosphoenolpyruvate carboxylase from cultured tobacco cells. Plant Mol Biol 17: 535–539 (1991).
Kozak M: Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev 47: 1–45 (1983).
Latzko E, Kelly GJ: The many-faceted function of phosphoenolpyruvate carboxylase in C3 plants. Physiol Vég 21: 805–815 (1983).
Lepiniec L, Santi S, Keryer E, Amiet V, Vidal J, Gadal P, Cretin C: Complete nucleotide sequence of one member of the Sorghum phosphoenolpyruvate carboxylase gene family. Plant Mol Biol 17: 1077–1079 (1991).
O'Leary MH: Phosphoenolpyruvate carboxylase: an enzymologist's view. Annu Rev Plant Physiol 33: 297–315 (1982).
Rickers J, Cushman JC, Michalowski CB, Schmitt JM, Bohnert HJ: Expression of the CAM-form of phospho(enol)pyruvate carboxylase and nucleotide sequence of a full length cDNA from Mesembryanthemum crystallinum. Mol Gen Genet 215: 447–454 (1989).
Sugimoto T, Tanaka K, Monma M, Kawamura Y, Saio K: Phosphoenolpyruvate carboxylase level in soybean seed highly correlates to its contents of protein and lipid. Agric Biol Chem 53: 885–887 (1989).
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Sugimoto, T., Kawasaki, T., Kato, T. et al. cDNA sequence and expression of a phosphoenolpyruvate carboxylase gene from soybean. Plant Mol Biol 20, 743–747 (1992). https://doi.org/10.1007/BF00046459
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DOI: https://doi.org/10.1007/BF00046459