Summary
A high level of activity of a β-1,3-glucan hydrolase is present in leaves of Nicotiana glutinosa and the enzyme is also present in the roots, midribs, petioles and stems. By comparison, very low levels of β-1,4-glucan hydrolase are found throughout the plant. The activity of the β-1,3-glucan hydrolase in leaves aged on the plant was found to increase 14-fold during the course of leaf senescence and to reach a maximum in yellow-green leaves. Detached leaves and leaf discs floated on water in the dark showed similar patterns of change.
The increase in β-1,3-glucan hydrolase activity during senescence is apparently not due to the loss of an inhibitor from young green leaves or to the formation of an enzyme activator in yellow leaves. The enzyme in yellow leaves was electrophoretically indistinguishable from that in green leaves. The hydrolase is not firmly attached to the cell walls and is not present in the particulate fraction sedimenting at 105400xg for 60 min. Within the leaf cell it is therefore likely to be located either in the cytoplasm or in an easily disrupted structure such as a vacuole.
The relationship of the hydrolase to leaf senescence was investigated by examining the effect of plant hormones on the changes in level of hydrolase, protein and chlorophyll in leaf discs during senescence. IAA (10 μM) and GA3 (50 μM) did not alter the normal patterns of change, whilst Kin (50 μM) delayed the loss of protein and chlorophyll and also delayed and decreased the rise in hydrolase activity. In contrast, ABA (190 μM) which increased the rate of loss of protein and chlorophyll, also caused a decrease in the rate and extent of the rise in hydrolase.
Possible functions of the hydrolase in the leaf are discussed.
Similar content being viewed by others
Abbreviations
- CM-pachyman:
-
carboxymethyl pachyman
- CM-cellulose:
-
carboxymethyl cellulose
- BSA:
-
bovine serum albumin
- ABA:
-
abscisic acid
- GA3 :
-
gibberellic acid
- IAA:
-
indole-3-acetic acid
- Kin:
-
kinetin
References
Abeles, F. B.: Abscission: Role of Cellulase. Plant Physiol. 44, 447–452 (1969).
Abeles, F. B., Forrence, L. E.: Temporal and hormonal control of β-1,3-glucanase in Phaseolus vulgaris L. Plant Physiol. 45, 395–400 (1970).
Abeles, F. B., Leather, G. R.: Abscission: Control of cellulase secretion by ethylene. Planta (Berl.) 97, 87–91 (1971).
Addicott, F. T., Lyon, J. L.: Physiology of abscisic acid and related substances. Ann. Rev. Plant Physiol. 20, 139–164 (1969).
Atkin, R. K., Srivastava, B. I. S.: The changes in soluble protein of excised barley leaves during senescence and kinetin treatment. Physiol. Plantarum (Copenh.) 22, 742–750 (1969).
Atkin, R. K., Srivastava, B. I. S.: Studies on protein synthesis in senescing and kinetin-treated barley leaves. Physiol. Plantarum (Copenh.) 23, 304–315 (1970).
Balz, H. P.: Intracelluläre Lokalisation und Funktion von hydrolytischen Enzymen bei Tabak. Planta (Berl.) 70, 207–236 (1966).
Bean, R. C., Ordin, L.: A study of procedures for isolation and fractionation of plant cell walls. Analyt. Biochem. 2, 544–557 (1961).
Clarke, A. E., Stone, B. A.: β-1,3-Glucan hydrolases from the grape vine (Vitis vinifera) and other plants. Phytochemistry 1, 175–188 (1962).
Connell, G. E., Dixon, G. H., Hanes, C. S.: Quantitative chromatographic methods for the study of enzymic transpeptidation reactions. Canad. J. Biochem. 33, 416–427 (1955).
Currier, H. B., Shih, C. Y.: Sieve tubes and callose in Elodea leaves. Amer. J. Bot. 55, 145–152 (1968).
Datko, A. H., Maclachlan, G. A.: Indoleacetic acid and the synthesis of glucanases and pectic enzymes. Plant Physiol. 43, 735–742 (1968).
Davies, E., Maclachlan, G. A.: Effects of indoleacetic acid on intracellular distribution of β-glucanase activities in the pea epicotyl. Arch. Biochem. Biophys. 128, 595–600 (1968).
De Leo, P., Sacher, J. A.: Control of ribonuclease and acid phosphatase by auxin and abscisic acid during senescence of Rhoeo leaf sections. Plant Physiol. 46, 806–811 (1970).
Eschrich, W.: Kallose. Protoplasma 47, 487–530 (1956).
Eschrich, W.: Biochemistry and fine structure of phloem in relation to transport. Ann. Rev. Plant Physiol. 21, 193–214 (1970).
Esser, K.: Bildung und Abbau von Callose in den Samenanlagen der Petunia hybrida. Z. Biol. 57, 32–51 (1963).
Frankel, R., Izhar, S., Nitsan, J.: Timing of callase activity and cytoplasmic male sterility in Petunia. Biochem. Genet. 3, 451–455 (1969).
Goa, J.: A micro Biuret method for protein determination. Scand. J. clin. Lab. Invest. 5, 218–222 (1953).
Jones, R. L.: Gibberellic acid-enhanced release of β-1,3-glucanase from barley aleurone cells. Plant Physiol. 47, 412–416 (1971).
Lewis, L. N., Varner, J. E.: Synthesis of cellulase during abscission of Phaseolus vulgaris leaf explants. Plant Physiol. 46, 194–199 (1970).
MacLeod, A. M., Duffus, J. H., Johnston, C. S.: Development of hydrolytic enzymes in germinating grain. J. Inst. Brew. 70, 521–528 (1964).
Maizel, J. V.: Acrylamide-gel electrophoretograms by mechanical fractionation: Radioactive adeno-virus proteins. Science 151, 988–990 (1966).
Matile, P.: Enzyme der Vakuolen aus Wurzelzellen von Maiskeimlingen. Z. Naturforsch. 21 B, 871–878 (1966).
Matile, P.: Lysosomes of root tip cells in corn seedlings. Planta (Berl.) 79, 181–196 (1968).
Matile, P., Balz, J. P., Semadeni, E., Jost, M.: Isolation of spherosomes with lysosome characteristics from seedlings. Z. Naturforsch. 20 B, 693–698 (1965).
McHale, J. S., Dove, L. D.: Ribonuclease activity in tomato leaves as related to development and senescence. New Phytol. 67, 505–515 (1968).
McNairn, R. B., Currier, H. B.: The influence of boron on callose formation in primary leaves of Phaseolus vulgaris. Phyton (B. Aires) 22, 153–158 (1965).
McNairn, R. B., Currier, H. B.: Translocation blockage by sieve plate callose. Planta (Berl.) 82, 369–380 (1968).
Mittelheuser, C. J., van Steveninck, R. F. M.: Ultrastructural changes in naturally senescing leaves compared with changes induced by (RS)-abscisic acid. Plant growth substances, 1970. Carr, D. J., ed., New York: Plenum 1972 (In press).
Moore, A. E., Stone, B. A.: The occurrence of a β-1,3-glucan hydrolase in plants of Nicotiana glutinosa in normal and pathological states. Proc. Federation European Biochem. Soc., Prague, p. 182, 1968.
Moore, A. E., Stone, B. A.: A β-1,3-glucan hydrolase from Nicotiana glutinosa leaves. I. Extraction, purification and physical properties. Biochim. biophys. Acta (Amst.) 258, 238–247 (1972a).
Moore, A. E., Stone, B. A.: A β-1,3-glucan hydrolase from Nicotiana glutinosa Leaves. II. Specificity, action pattern and inhibitor studies. Biochim. biophys. Acta (Amst.) 258, 248–264 (1972b).
Ratner, A., Goren, R., Monselise, S. P.: Activity of pectin esterase and cellulase in the abscission zone of citrus leaf explants. Plant Physiol. 44, 1717–1723 (1969).
Reese, E. T., Mandels, M.: Enzymatic hydrolysis of β-glucans. In: Advances in enzymic hydrolysis of cellulose and related materials, p. 197–234, Reese, E. T., ed., Oxford: Pergamon 1963.
Semadeni, E. G.: Enzymatic characterization of lysosome equivalents (spherosomes) in corn seedlings. Planta (Berl.) 72, 91–118 (1967).
Taiz, L., Jones, R. L.: Gibberellic acid, β-1,3-glucanase and the cell walls of barley aleurone layers. Planta (Berl.) 92, 73–84 (1970).
Whatley, F. R., Arnon, D. T.: Photosynthetic phosphorylation in plants. Methods in Enzymol. 6, 308–313 (1963).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Moore, A.E., Stone, B.A. Effect of senescence and hormone treatment on the activity of a β-1,3-glucan hydrolase in Nicotiana glutinosa leaves. Planta 104, 93–109 (1972). https://doi.org/10.1007/BF00386986
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00386986