Abstract
The content of ATP, ADP, AMP, Pi, the activity of the enzymes involved in the glycolytic pathway, some problems of their regulation by adenine nucleotides and some basic problems connected with tissue energy balance were studied in tobacco plants infected with the potato virus Y (PVY). The contents of ATP and ΣAdN were increased in virus-infected tissues when compared with healthy tissues and correlated with the PVY reproduction curve. ADP and AMP contents decreased just after the inoculation and increased at the end of the experimental period, Pi content was not influenced by the infection.
The activities of the key enzymes of the glycolytic pathway (6-phosphofructokinase, hexosediphosphatase, and pyruvate kinase), determined both in crude homogenates and after partial purification, did not differ during the entire experimental period from the values found in healthy control tissues, similarly as the activities of glucosephosphate isomerase, glyceraldehydephosphate dehydrogenase, phosphoglyceromutase and enolase observed in crude homogenates. The unchanging AEC value in virus-infected tissues simultaneously indicated that no change in the rate of the glycolytic pathway occurred even under “invivo” conditions at the period of the acute stage of infection.
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References
Atkinson, D. E., Walton, G. M.: Adenosine triphosphate conservation in metabolic regulation. - J. biol. Chem.242: 3239–3241, 1967.
Bergman, E. L., Boyle, J. S.: Effect of tobacco mosaic virus on the mineral content of tomato leaves. -Phytopathology52: 956–957, 1962.
Black, C. C., Humphreys, T. E.: Effects of 2,4-dichlorophenoxyacetic acid on enzymes of glycolysis and pentose phosphate cycle. - Plant. Physiol.37: 66–73, 1962.
Boser, H.: Einfluss pflanzlicher Virosen auf Stoffwechselfunktionen des Wirtes. - Phytopathol. Z.37: 164–169, 1959.
Bozarth, R. F., Browning, R. E.: Effect of infection with southern bean mosaic virus and the diurnal cycle on the free nucleotide pool of bean leaves. - Phytopathology60: 852–855, 1970.
Bradford, M. M.: 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.
Cole, C. V., Ross, C.: Extraction, separation and quantitative estimation of soluble nucleotides and sugar phosphates in plant tissues. - Anal. Biochem.17: 526–539, 1966.
Esanu, V.: Contributions to the study of TMV influence on phosphorus metabolism-energetic metabolism relationship. -Phytopathol. Z.64: 221–241, 1969.
Esanu, V., Såvulescu, A.: Some aspects of the metabolism of host-parasite relationship in the case of T.M.V. - Phytopathol. Z.59: 347–351, 1967.
Huth, W.: Das Verhalten einiger Enzyme des Kohlenhydratstoffwechsels in Kartoffel-X-Virus-kranken Tabakpflanzen. -Phytopathol. Z.77: 117–124, 1973.
Jirácek, V., Kanta, J., Votruba, I., Kryzánek, R.: [Systematic analysis of fundamental types of phosphorus compounds in plant material.] In Czech. - Rostlinná Výroba (Praha)13: 249–266, 1967.
Kapur, S. P., Gumpf, D. J., Weathers, L. G.: Some effects of metabolic changes induced in “Etrog” citron by three isolates of exocortis virus. - Phytopathology64: 196–201, 1974.
Kelly, G. J., Turner, J. F.: The regulation of pea-seed phosphofructokinase by phosphoenolpyruvate. - Biochem. J.115:481–487, 1969.
Kelly, G. J., Turner, J. F.: The regulation of pea-seed phosphofructokinase by 6-phosphogluconate, 3-phosphoglycerate, 2-phosphoglycerate, and phosphoenolpyruvate. - Biochim. biophys. Acta208: 360–367, 1970.
Kozlowska, A.: Enzymic hydrolysis of adenosine triphosphate by healthy, virus X and TMV (tobacco mosaic virus) infected tobacco and tomato plants. - Acta biol. cracov. Ser. Bot.10: 207–216, 1967.
Ladygina, M. E., Rubin, B. A., Tukeeva, M. I.: Effect of tobacco mosaic virus on energy metabolism of tobacco species differing in respect to resistivity. - Sov. Plant Physiol.13: 780–784, 1966.
Makovcová, O., Sindelár, L.: Durch TMV-Infektion hervorgerufene Veränderung der Intensität der Glycolyse und des Pentosephosphatcyclus bei Tabakpflanzen. - Biol. Plant.19: 253–258, 1977.
Makovcová, O., Sindelár, L.: The effect of 2,4-dichlorophenoxyacetic acid on the metabolic utilization of free carbohydrates in cucumber mosaic virus infected cucumber plants. - Biol. Plant.23: 465–468, 1981.
Makovcová, O., Sindelár, L., HanuSová, M.: [Spectrophotometric determination of reproduction curves of TMV, PVY and CMV in tobacco and of CMV in cucumber.] In Czech. - Sbor. ÚVTIZ-Ochrana Rostlin (Praha)14: 17–24, 1978.
Makovcová, O., Sindelár, L., HanuSová, M.: [Saccharose metabolism in leaves of cucumber infected by cucumber mosaic virus as related to yields.] In Czech. - Sbor. ÚVTIZ - Ochrana Rostlin (Praha)16: 263–269, 1980.
Nakayama, H., Fuii, M., Miura, K.: Partial purification and some regulatory properties of pyruvate kinase from germinating castor bean endosperm. - Plant Cell Physiol.17: 653–660, 1976.
Rebowska, Z.: [Changes in metabolism of TMV (tobacco mosaic virus) infected tomato plants.] In Pol. - Zesz. probl. Post. Nauk roln.111: 165–167, 1971.
Rodwell, V. M., Townb, J. C., Grisolia, S.: Bestimmung der 3-Phosphoglycerinsäuremutase.- Biochim. Biophys. Acta20: 394–399, 1956.
Sagisaka, S., Asada, M.: Coordinate and noncoordinate changes in enzyme activities in pentose phosphate cycle in poplar: a control of enzyme activities in differentiated xylem. - Plant Cell Physiol.22: 1459–1468, 1981.
Sasaki, K., Hirai, T.: Changes in the amounts of phosphorus compounds of tobacco leaves infected with tobacco mosaic virus, with special reference to the effect of dinitrophenol. - Phytopathol. Z.46: 343–350, 1963.
Solymosy, F., Farkas, G. L.: Metabolic characteristics at the enzymatic level of tobacco tissues exhibiting localized acquired resistance to viral infection. - Virology21: 210–221, 1963.
Sunderland, D. W., Merrett, M. J.: Adenosine diphosphate and adenosine triphosphate concentrations in leaves showing necrotic local virus lesions. - Virology23: 274–276, 1964.
Sunderland, D. W., Merrett, M. J.: Respiration rate, adenosine diphosphate and triphosphate concentrations of leaves showing necrotic local lesions following infection by tobacco mosaic virus. - Physiol. Plant.20: 368–372, 1967.
Sindelár, L.: [The changes in metabolic utilization of free saccharides and starch in potato Y-virus infected tobacco.] In Czech. - Ph. D. Thesis, Charles Univ., Praha 1972.
Sindelár, L.: [Some changes in metabolic utilization of free carbohydrates and starch in potato Y-virus infected tobacco.] In Czech. - CSc. Thesis, Czechosl. Acad. Sci., Praha 1984.
Sindelár, L.: Changes in the activity of glueose-6-phosphate dehydrogenase and some problems relating to its regulation in tobacco plants infected with potato virus Y. - Biol. Plant.28: 440–448, 1986.
Sindelár, L., Makovcová, O.: Beziehungen zwischen der Phosphatasen-Aktivität und dem Gehalt der freien Zucker bei durch die Strichelkrankheit der Kartoffeln infiziertemN. tabacum cv. “Samsun”. - Biol. Plant.16: 376–381, 1974.
Taniguchi, T.: A rapid method for microanalytical determination of the amount of tobacco mosaic virus in plant tissues. -Nature194: 708, 1962.
Thilo, H. J., Nienhaus, F.: Stoffwechselphysiologische Veränderungen in der Pflanze nach Virusinfektion unter Einfluss von Wundreiz. - Phytopathol. Z.76: 97–107, 1973.
Turner, J. F., Turner, D. H.: The regulation of glycolysis and the pentose phosphate pathway. - In:Davies, D. (ed.): The Biochemistry of Planta. Vol. 2. Pp. 297 - 312. Academic Press, New York-London -Toronto-Sydney-San Francisco 1980.
Weintraub, M., Ragetli, H. W., Lo, E.: Mitochondrial content and respiration in leaves with localized virus infections. - Virology50: 841–850, 1972.
Woodrow, I. E., Kelly, G. J., Latzko, E.: Fructosebisphosphatase of plant roots. - Z. Pflanzenphysiol.106: 119–127, 1982.
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Sindelár, L. The content of ATP, ADP, AMP, Pi, the activity of enzymes involved in the glycolytic pathway and some problems of its regulation, and energy balance in tobacco plants infected with potato virus Y. Biol Plant 28, 449–459 (1986). https://doi.org/10.1007/BF02885049
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DOI: https://doi.org/10.1007/BF02885049