Abstract
Tryptophan decarboxylase (EC 4.2.1.27) is synthesized de-novo by Catharanthus roseus cells shortly after the cells have been transferred into culture medium in which monoterpenoid indole alkaloids are formed. The enzyme production, monitored by in-vivo labelling with [35S]methionine and immunoprecipitation, precedes the apparent maximal enzyme activity by 10–12 h. From the time course of the descending enzyme activity after induction, a half-life of 21 h for tryptophan decarboxylase in C. roseus cell suspensions is calculated. A comparison of the polyadenylated-RNA preparations from C. roseus cells indicates that mRNA activity for tryptophan decarboxylase is only detected in cells grown in the production medium. The importance of tryptophan decarboxylase induction with respect to the accumulation of th corresponding alkaloids is discussed.
Similar content being viewed by others
Abbreviations
- TDC:
-
tryptophan decarboxylase
References
Berlin, J., Forche, E., Wray V., Hammer, J., Hösel, W. (1983) Formation of benzophenanthridine alkaloids by suspension cultures of Eschscholtzia california. Z. Naturforsch. Teil C 38, 346–352
Bradford, 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, 2488–2492
Engvall, E. (1980) Enzyme immunoassay ELISA and EMIT. Methods Enzymol. 70, 419–439
Fujita, Y., Hara, Y., Suga, C., Morimoto, T. (1981) Production of shikonin derivatives by cell suspension cultures of Lithospermum erythrorhizon. Plant Cell Rep. 1, 61–63
Heller, W., Egin-Bühler, B., Gardiner, S., Knobloch, K.-H., Matern, U., Ebel, J., Hahlbrock, K. (1979) Enzymes of general phenylpropanoid metabolism and of flavonoid glycoside biosynthesis in parsley. Plant Physiol. 64, 371–373
Kabat, E.A., Mayer, M.M. (1967) Immunological and immunochemical methodology. In: Experimental immunochemistry, 3rd edn., pp. 22–97, Thomas, C.C., ed., Springfield, Illinois, USA
Knobloch, K.-H., Berlin, J. (1980) Influence of medium composition on the formation of secondary compounds in cell suspension cultures of Catharanthus roseus (L.) G. Donn. Z. Naturforsch. Teil C 35, 551–556
Knobloch, K.-H., Berlin, J. (1981) Phosphate mediated regulation of cinnamoyl putrescine biosynthesis in cell suspension cultures of Nicotiana tabacum. Planta Med. 42, 167–172
Knobloch, K.-H., Berlin, J. (1983) Influence of phosphate in the formation of indole alkaloids and phenolic compounds in cell suspension cultures of Catharanthus roseus. I. Comparison of enzyme activities and product accumulation. Plant Cell Tiss. Org. Cult. 2, 333–340
Knobloch, K.-H., Hansen, B., Berlin, J. (1981) Medium-induced formation of indole alkaloids and concomitant changes of interrelated enzyme activities in cell suspension cultures of Catharanthus roseus. Z. Naturforsch. Teil C 36, 40–43
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685
Maizel, J.V. (1971) Polyacrylamide gel electrophoresis of viral proteins. Methods Virol. 5, 170–246
Maniatis, T., Fritsch, F.G., Sambrook, J. (1982) Molecular cloning: A laboratory manual. Biol. Lab., Cold Spring Harbor
Mantell, S.H., Pearson, D.W., Hazell, L.P., Smith, H., (1983) The effect of initial phosphate and sucrose levels on nicotine accumulation in batch suspension cultures of Nicotiana tabacum L. Plant Cell Rep. 2, 73–77
Mizukami, H., Nordlöv, H., Lee, S.-L., Scott, A.J. (1979) Purification and properties of strictosidine synthase (an enzyme condensing tryptamine and secologanin) from Catharanthus roseus cultured cells. Biochemistry 17, 3760–3763
Noé, W., Mollenschott, C., Berlin, J. (1984) Tryptophan decarboxylase from Catharanthus roseus cell suspension cultures. Purification, molecular and kinetic data of the homogeneous protein. Plant Mol. Biol. 3, 281–288
Ouchterlony, ö (1949) Antigen-antibody reactions in gel. Acta Pathol. Microbiol. Scand. 25, 507–515
Sasse, F., Buchholz, M., Berlin, J. (1983) Selection of cell lines of Catharanthus roseus with increased tryptophan decarboxylase activity. Z. Naturforsch. Teil C 38, 916–922
Sasse, F., Heckenberg, U., Berlin, J. (1982a) Accumulation of β-carboline alkaloids and serotonin by cell cultures of Peganum harmala. II. Interrelationship between accumulation of serotonin and activities of related enzymes. Z. Pflanzenphysiol. 105, 315–322
Sasse, F., Knobloch, K.-H., Berlin, J. (1982b) Induction of secondary metabolism in cell suspension cultures of Catharanthus roseus, Nicotiana tabacum and Peganum harmala. In: Plant tissue culture 1982 pp. 343–344, Fujiwara, A., ed. Maruzen Co. Ltd., Tokyo, Japan
Schimke, R.T. (1974) Protein synthesis and degradation in animal tissues. MTP Int. Rev. Science, Biochem. Ser. I, vol. 9, pp. 183–221, Paul, J., ed. Butterworth London
Schröder, G., Schröder, J. (1982) Hybridization selection and translation of T-DNA encoded mRNAs from octopine tumors. Mol. Gen. Genet. 185, 51–55
Stoeckigt, J., Zenk, M.-H. (1977) Isovincoside (strictosidine), the key intermediate in the enzymatic formation of indole alkaloids. FEBS Lett. 79, 233–237
Towbin, H., Staehelin, T., Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some application Proc. Natl. Acad. Sci. USA 76, 4350–4353
Treimer, J.F., Zenk M.-H. (1979) Purification and properties of strictoside synthase, the key enzyme in indole alkaloid formation. Eur. J. Biochem. 101, 225–233
Zenk, M.-H. (1980) Enzymatic synthesis of ajmalicine and related indole alkaloids. J. Nat. Prod. 43, 438–451
Zenk, M.-H., El-Shagi, HL., Arens, H., Stoeckigt, J., Weiler, E.W., Deus, B. (1977) Formation of the indole alkaloids serpentine and ajmalicine in cell suspension cultures of Catharanthus roseus In: Plant tissue culture and its biotechnological application, pp. 27–42, Barz, W., Reinhard, E., Zenk, M.H., eds. Springer, Berlin Heidelberg New York
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Noé, W., Berlin, J. Induction of de-novo synthesis of tryptophan decarboxylase in cell suspensions of Catharanthus roseus . Planta 166, 500–504 (1985). https://doi.org/10.1007/BF00391274
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00391274