Abstract
Thioglucoside glucohydrolase (EC 3.2.3.1; myrosinase) hydrolyses glucosinolates and thereby liberates glucose and sulphur and nitrogen compounds. To examine the hypothesis that the myrosinase-glucosinolate system is influenced by environmental factors, the effect of sulphate on the expression of myrosinases was examined. On examining different plant organs at various stages, it was observed that sulphate induces a differential expression of myrosinase polypeptides in plants ofSinapis alba L. (white mustard). Specific myrosinase polypeptides, dependent on sulphate in the growth medium, were detected on immunoblots. Without sulphate a maximum of three polypeptides was detected in buds, two in cotyledons and one in stems and roots. In plants cultured on medium with sulphate up to four polypeptides could be observed in cotyledons, five polypeptides in buds, two in stems and one in roots. Expression of myrosinases was, in general, high in plants cultured on a medium supplemented with sulphate. In floweringS. alba plants, sulphate-starved plants showed a higher expression of myrosinase in cotyledons and stems compared to plants fed with sulphate. Sulphate-fed plants had a high expression in inflorescences and roots. The organ- and time-specific induction of the myrosinase expression is discussed in relation to sulphate metabolism and availability of sulphate under normal conditions of cultivation and in relation to protection of Brassicaceae species. This is the first evidence for a specific induction of individual myrosinase proteins.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- IEF:
-
isoelectricfocusing
- MS-medium:
-
Murashige and Skoog medium
- pI:
-
isoelectric point
References
Bell, C.I., Cram, W.J., Clarkson, D.T. (1990) Turnover of sulphate in leaf vacuoles limits retranslocation under sulphur stress. In. Sulphur nutrition and sulphur assimilation in higher plants, pp. 163–165, Rennenberg, H., Brunold, C., de Kok, L.J., Stulen, I., eds. SPB Academic Publishing, Hague
Bones, A.M. (1990) Distribution of β-thioglucosidase activity in intact plants, cell and tissue cultures and regenerated plants ofBrassica napus L. J. Exp. Bot.41, 737–744
Bones, A.M., Espevik, T. (1987) Monoclonal antibodies to myrosinase in plants. Proc. 7th Int. Rapeseed Congr., 6, pp. 1482–1489, Poznan, Poland
Bones, A.M., Iversen, T.-H. (1985) Myrosin cells and myrosinase. Isr. J. Bot.34, 351–375
Bones, A.M., Slupphaug, G. (1989) Purification, characterization and partial amino acid sequencing of β-thioglucosidase fromBrassica napus L. J. Plant Physiol.134, 722–729
Bones, A.M., Thangstad, O.P. (1991) Preparative purification of myrosinase fromSinapis alba L. — Characterization of polyclonal antibodies against myrosinase. Proc. 8th Int. Rapeseed Congr., 3, pp. 899–904, McGregor, D.I., ed. Saskaaton, Canada
Bones, A.M., Thangstad, O.P., Haugen, O.A., Espevik, T. (1991) Fate of myrosin cells: Characterization of monoclonal antibodies against myrosinase. J. Exp. Bot.42, 1541–1549
Bradford, M.M. (1976) 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
Chadchawan, S., Bishop, J., Thangstad, O.P., Bones, A.M., Mitchell-Olds, T., Bradley, D. (1993)Arabidopsis cDNA sequence encoding myrosinase. Plant Physiol.103, 671–672
Chew, F.S. (1988) Biological effects of glucosinolates. In: Biologically active natural products for potential use in agriculture, pp. 155–181, Cutler, H.G., ed. Am. Chem. Soc., Washington
Evans, L.T. (1975) Sulphur in agriculture. In: Sulphur in australasian agriculture, pp. 3–9, McLachlan, K.D., ed. U.P. Sydney
Fenwick, G.R., Heaney, R.K., Mullin, D.J. (1983) Glucosinolates and their breakdown products in food and food plants, Crit. Rev. Food Sci. Nutr.18, 123–201
Grob, R., Matile, P. (1979) Vacuolar location of glucosinolates in horseradish root cells. Plant Sci. Lett.14, 327–335
Heukeshoven, J., Dernick, R. (1985) Simplified method for silver staining in polyacrylamide gels and the mechanism of silver staining. Electrophoresis6, 103–112
Höglund, A.-S., Lenman, M., Falk, A., Rask, L. (1991) Distribution of myrosinase in rapeseed tissues. Plant Physiol.95, 213–221
Höglund, A.-S., Lenman, M., Rask, L. (1992) Myrosinase is localized to the interior of myrosin grains and is not associated to the surrounding tonoplast membrane. Plant Sci.85, 165–170
James, D., Rossiter, J.T. (1991) Development and characteristics of myrosinase inBrassica napus during early seedling growth. Physiol. Plant.82, 163–170
Koritsas, V.M., Lewis, J.A., Fenwick, G.R. (1989) Accumulation of indole glucosinolates inPsylliodes chrysocephala L.-infested, or-damaged tissues of oilseed rape (Brassica napus L.) Experientia45, 493–495
Lenman, M., Rödin, J., Josefsson, L.-R., Rask, L. (1990) Immunological characterization of rapeseed myrosinase. Eur. J. Biochem.194, 747–753
MacGibbon, D.B., Allison, R.M. (1970) A method for the detection of plant glucosinolases (myrosinases). Phytochemistry9, 541–544
Machev, N.P., Schraudolf, H. (1978) Thiocyanate as predecessor of asparagine inSinapis alba L. Plant Physiol. (Bulgaria)4, 26–33
Matile, P. (1980) “Die Senfölbombe”: Zur Kompartimentierung des Myrosinasesystems. Biochem. Physiol. Pflanz.175, 722–731
Murashige, T., Skoog, F. (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant.15, 473–497
Raven, J.A. (1980) Nutrient transport in microalgae. Adv. Microbial. Physiol.21, 47–226
Schnug, E. (1990) Glucosinolates-fundamental, environmental and agricultural aspects. In: Sulphur nutrition and sulphur assimilation in higher plants, pp. 97–106, Rennenberg, H., Brunold, C., de Kok, L.J., Stulen, I., eds. SPB Academic Publishing, Hague
Syers, J.K., Skinner, R.J., Curtin, D. (1987) Soil and fertiliser sulphur in U.K. agriculture. Proc. Fert. Soc.264, 1–43
Thangstad, O.P., Iversen, T.H., Slupphaug, G., Bones, A.M. (1990) Immunocytochemical localization of myrosinase inBrassica napus L Planta180, 245–248
Thangstad, O.P., Evjen, K., Bones, A.M. (1991) Immunogold-EM localization of myrosinase in Brassicaceae. Protoplasma161, 85–93
Thangstad, O.P., Winge, P., Husebye, H., Bones, A.M. (1993) The myrosinase (thioglucoside glucohydrolase) gene family in Brassicaceae. Plant Mol. Biol.23, 511–524
Wei, X., Roomans, G.M., Sevéus, L., Pihakaski, K. (1981) Localization of glucosinolates in roots ofSinapis alba using X-ray microanalysis. Scanning Electron. Microsc.2, 481–488
Xue, J., Lenman, M., Falk, A., Rask, L. (1992) The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family: Plant Mol. Biol.18, 387–398
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bones, A.M., Visvalingam, S. & Thangstad, O.P. Sulphate can induce differential expression of thioglucoside glucohydrolases (myrosinases). Planta 193, 558–566 (1994). https://doi.org/10.1007/BF02411562
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02411562