Abstract
Anaerobiosis rapidly induces alcohol dehydrogenase (ADH), an enzyme of the fermentation pathway, in different parts of rice seedlings. After initiation of anaerobiosis, the activity of the enzyme increases linearly for 3 days or more. The ADH activity is anaerobically inducible even in mature rice leaves in contrast to maize which shows no induction in mature leaves. Rice ADH activity can also be induced by an auxin analog, 2,4-dichlorophenoxyacetic acid, under aerobic conditions. The experimental results show that anaerobiosis increases the ADH mRNA level, indicating that the ADH enzyme is regulated at the transcriptional level. Starch gel electrophoresis of a protein extract from rice shows 3 distinct forms of ADH. The amounts of the 3 forms vary with the organ, suggesting that the expression of ADH genes is organ-specific. Sequencing data show that the two different cloned cDNA copies of ADH mRNAs are derived from two different genes.
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References
Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254 (1976).
Chang C, Meyerowitz EM: Molecular cloning and DNA sequence of Arabidopsis thaliana alcohol dehydrogenase gene. Proc Natl Acad Sci USA 83: 1408–1412 (1986).
Chirgwin JJ, Przbyla AE, MacDonald RJ, Rutter WS: Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18: 5794 (1979).
Cobb BG, Kennedy RA: Distribution of alcohol dehydrogenase in roots and shoots of rice and Echinochloa seedlings. Plant, Cell & Environment 10: 633–638 (1987).
Dennis ES, Gerlach WL, Pryor AJ, Bennetzen JL, Inglis A et al.: Molecular analysis of the alcohol dehydrogenase (Adh1) gene of maize. Nucleic Acids Res 12: 3983–4000 (1984).
Dennis ES, Sachs MM, Gerlach WL, Finnegan EJ, Peacock WJ: Molecular analysis of the alcohol dehydrogenase-2 (Adh2) gene of maize. Nucleic Acids Res 13: 727–743 (1985).
Eliasson L: Growth response of wheat roots to antiauxins and 2,3.5-thiiodobenzoic acid. Physiol Plant 6: 451 (1960).
Eklund H, Nordstrom B, Branden CI: Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. J Mol Biol 102: 27–59 (1976).
Fluhr R, Kuhlemeier C, Nagy F, Chua N-H: Organspecific and light-induced expression of plant genes. Science 232: 1106–1111 (1986).
Freeling M: Simultaneous induction by anaerobiosis or 2,4-D of multiple enzymes specified by two unlinked genes: differential ADH1-ADH2 expression in maize. Mol Gen Genet 127: 215–227 (1973).
Freeling M, Bennett DC: Maize Adh1. Ann Rev Genet 19: 297–323 (1985).
Gerlach WL, Pryor AJ, Dennis ES, Ferl RJ, Sachs MM, Peacock WJ: cDNA cloning and induction of the alcohol dehydrogenase gene (Adh1) of maize. Proc Natl Acad Sci USA 79: 2981–2985 (1982).
Gottlieb LP: Conservation and duplication of isozymes in plants. Science 216: 373–380 (1982).
Hanson AD, Jacobsen JV, Zwar JA: Regulated expression of three alcohol dehydrogenase genes in barley aleurone layers. Plant Physiol 75: 573–581 (1984).
Huynh TV, Yong RA, Davis RW: Constructing and screening cDNA libraries in λgt10 and λgt11. In: Glover DM (ed) DNA Cloning, vol. 1, pp. 49–78. IRL Press, Oxford Washington, DC (1985).
Joshi CP: Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis. Nucleic Acids Res 15: 9627–9640 (1987).
Kadowaki KI, Matsuoka M, Murai N, Harada K: Induction of two alcohol dehydrogenase polypeptides in rice roots during anaerobiosis. Plant Sci 54: 29–36 (1988).
Laemmili UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685 (1970).
Lehrack H, Diamond D, Wozney JM, Boedtker M: RNA molecular weight determinations by gel electrophoresis under denaturing conditions: a critical reexamination. Biochemistry 16: 4743–4751 (1977).
Llewellyn DJ, Finnegan EJ, Ellis JG, Dennis ES, Peacock WJ: Structure and expression of an alcohol dehydrogenase 1 gene from Pisum sativum. J Mol Biol 195: 115–123 (1987).
Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1982).
McDevitt MA, Imperiale MJ, Ali H, Nevin JR: Requirement of a downstream sequence for generation of a poly(A) addition site. Cell 37: 993–999 (1984).
Mocquot B, Prat C, Mouches C, Pradet A: Effect of anoxia on energy charge and protein synthesis in rice embryo. Plant Physiol 68: 636–640 (1981).
Okimoto R, Sachs MM, Porter EK, Freeling M: Patterns of polypeptide synthesis in various maize organs under anaerobiosis. Planta 150: 89–94 (1980).
Phillips IDJ: Root-shoot hormone relations. II. Changes in endogenous auxin concentration produced by flooding of the root system in Helianthus annuus. Annals Bot 28: 37–45 (1964).
Queen C, Korn LJ: A comprehensive sequence analysis program for the IBM personal computer. Nucleic Acids Res 12: 581–599 (1984).
Ricard B, Mocquot B, Fournier A, Delseny M, Pradet A: Expression of alcohol dehydrogenase in rice embryos under anoxia. Plant Pol Biol 7: 321–329 (1986).
Sachs MM, Freeling M: Selective synthesis of alcohol dehydrogenase during anaerobic treatment of maize. Mol Gen Genet 161: 111–115 (1978).
Sachs MM, Freeling M, Okimoto R: The anaerobic proteins of maize. Cell 20: 761–767 (1980).
Sachs MM, Ho T-HD: Alteration of gene expression during environmental stress in plants. Ann Rev Plant Physiol 37: 363–376 (1986).
Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).
Schwartz D, Laughner WJ: A molecular basis for heterosis. Science 166: 626–227 (1969).
Schwartz D: Dimerization mutants of alcohol dehydrogenase of maize. Proc Natl Acad Sci USA 68: 145–164 (1971).
Shields CR, Orton TJ, Stuber CW: An outline of general resource needs and procedures for the electrophoretic separation of active enzymes from plant tissue. In: Tanksley SD, Orton TJ (eds) Isozymes in Plant Genetics and Breeding, Part A, pp. 443–467. Elsevier Science Publishers, Amsterdam (1983).
Shimomura S, Beevers H: Alcohol dehydrogenase and an inactivator from rice seedlings. Plant Physiol 71: 736–741 (1983).
Tanksley SD: Gene mapping. In: Tanksley SD, Orton TJ (eds) Isozymes in Plant Genetics and Breeding, Part A, pp. 109–138. Elsevier Science Publishers, Amsterdam (1983).
Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350–4354 (1979).
Trick M, Dennis ES, Edwards KJR, Peacock WJ: Molecular analysis of the alcohol dehydrogenase gene family of barley. Plant Mol Biol 11: 147–160 (1988).
Vartapetian BB, Andreeva IN, Nuritdinov N: Plant cells under oxygen stress. In: Donal DH, Crawford RMM (eds) Plant Life in Anaerobic Environments, pp. 13–88 (1978).
Yamada N: Auxin relationships of the rice coleoptile Plant Physiol 29: 92 (1954).
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Xie, Y., Wu, R. Rice alcohol dehydrogenase genes: anaerobic induction, organ specific expression and characterization of cDNA clones. Plant Mol Biol 13, 53–68 (1989). https://doi.org/10.1007/BF00027335
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DOI: https://doi.org/10.1007/BF00027335