Abstract
A cDNA clone containing a fructose-1,6-bisphosphate aldolase (ALD) gene, designated ClAldC, was isolated from the medicinal plant Codonopsis lanceolata. ClAldC is predicted to encode a precursor protein of 358 amino acid residues and its sequence shares high degrees of homology with a number of other ALDs. The expression of ClAldC in different C. lanceolata organs was analyzed using reverse transcriptase (RT)-PCR. The results showed that ClAldC is highly expressed in the stems of an intact plant, while expressed at low level in leaves and roots. In addition, the expression of ClAldC under different abiotic stresses was analyzed at different points in time. Three tested abiotic stimuli, i.e., anoxygenic stress, hydrogen peroxide, and chilling, triggered a significant induction of ClAldC within 2–8 h post-treatment. However, there was no induction under the other four stresses, i.e., NaCl, wounding, light, and dark. The positive responses of ClAldC to the three abiotic stimuli suggested that C. lanceolata ClAldC may help to protect against environmental stresses such as anoxia, chilling and oxidative stress.
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References
Rutter W.J. 1964. Evolution of aldolase. Fed. Proc. 23, 1248–1257.
Flechner A., Gross W., Martin W.F., Schnarrenberger C. 1999. Chloroplast class I and II aldolases are bifunctional for fructose-1,6-biphosphate and sedoheptulose-1,7-biphosphate cleavage in the Calvin cycle. FEBS Lett. 447, 200–202.
Konishi H., Yamane H., Maeshima M., Komatsu S. 2004. Characterization of fructose-bisphosphate aldolase regulated by gibberellin in roots of rice seedling. Plant Mol. Biol. 56, 839–848.
Lal A., Plaxton W.C., Kayastha A.M. 2005. Purification and characterization of an allosteric fructose-1,6-bisphosphate aldolase from germinating mung beans (Vigna radiata). Phytochemistry. 66, 968–974.
Koonin E.V., Galperin M.Y. 2002. Carbohydrate metabolism. In: Sequence-Evolution-Function. Ed. Koonin E.V. N.Y.: Kluwer.
Lebherz H.G., Rutter W.J. 1969. Distribution of fructose diphosphate aldolase variants in biological systems. Biochemistry. 8, 109–121.
Zgiby S.M., Thomson G.J., Qamar S., Berry A. 2000. Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose-1,6-bisphosphate aldolases. Eur. J. Biochem. 267, 1858–1868.
Buchanan B.B., Gruissem W., Jones R.L. 2005. Carbohydrate metabolism. In: Biochemistry and Molecular Biology of Plants. Eds. Buchanan B.B. et al. Rockville, MD, 630–675.
Weeden N.F., Gottlieb L.D. 1980. The genetics of chloroplast enzymes. J. Hered. 71, 392–396.
Plaxton W.C. 1996. The organization and regulation of plant glycolysis. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 185–214.
Han D.S. 1992. Saengyakhak. Seoul, Korea: Dongmyungsa, pp. 197–199.
Murashige T., Skoog F. 1962. A revised medium for rapid growth and bioassay with tobacco tissue culture. Physiol. Plant. 15, 473–497.
Lebherz H.G., Leadbetter M.M., Bradshaw R.A. 1984. Isolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose bisphosphate aldolase. J. Biol. Chem. 259, 1011–1017.
Kelley P.M., Freeling M. 1984. Anaerobic expression of maize fructose-1,6-diphosphate aldolase. J. Biol. Chem. 259, 14180–14183.
Kelley P.M., Tolan D.R. 1986. The complete amino acid sequence for the anaerobically induced aldolase from maize derived from cDNA clones. Plant Physiol. 82, 1076–1080.
Andrews D.L., MacAlpine D.M., Johnson J.R., Kelley P.M., Cobb B.G., Drew M.C. 1994. Differential induction of mRNAs for the glycolytic and ethanolic fermentative pathways by hypoxia and anoxia in maize seedlings. Plant Physiol. 106, 1575–1582.
Umeda M., Uchimiya H. 1994. Differential transcript levels of genes associated with glycolysis and alcohol fermentation in rice plants (Oryza sativa L.) under submergence stress. Plant Physiol. 106, 1015–1022.
Bucher M., Kuhlemeier C. 1993. Long term anoxia tolerance. Plant Physiol. 103, 441–448.
Minhas D., Grover A. 1999. Transcript levels of genes encoding various glycolytic and fermentation enzymes change in response to abiotic stresses. Plant Sci. 146, 41–51.
Yamada S., Komori T., Hashimoto A., Kuwata S., Imaseki H., Kubo T. 2000. Differential expression of plastidic aldolase genes in Nicotiana plants under salt stress. Plant Sci. 154, 61–69.
Zhang X.N., Wang H., Qu Z. C., Ye M.M., Shen D.L. 2002. Cloning and prokaryotic expression of a salt-induced cDNA encoding a chloroplastic fructose-1,6-diphosphate aldolase in Dunaliella salina (Chlorophyta). DNA Seq. 13, 195–202.
Taylor W.C. 1989. Transcriptional regulation by a circadian rhythm. Plant Cell. 1, 259–264.
Kagaya Y., Nakamura H., Hiaka S., Ejiri S., Tsutsumi K. 1995. The promoter from the rice nuclear gene encoding chloroplast aldolase confers mesophyll-specific and light-regulated expression in transgenic tobacco. Mol. Gen. Genet. 248, 668–674.
Hayama R., Izawa T., Shimamoto K. 2002. Isolation of rice genes possibly involved in the photoperiodic control of flowering by a fluorescent differential display method. Plant Cell Physiol. 43, 494–504.
Michelis R., Gepstein S. 2000. Identification and characterization of a heat-induced isoform of aldolase in oat chloroplast. Plant Mol. Biol. 44, 487–498.
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Published in Russian in Molekulyarnaya Biologiya, 2008, Vol. 42, No. 2, pp. 206–213.
The text was submitted by the authors in English.
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Purev, M., Kim, M.K., Samdan, N. et al. Isolation of a novel fructose-1,6-bisphosphate aldolase gene from Codonopsis lanceolata and analysis of the response of this gene to abiotic stresses. Mol Biol 42, 179–186 (2008). https://doi.org/10.1134/S0026893308020027
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DOI: https://doi.org/10.1134/S0026893308020027