Advertisement

Plant Cell, Tissue and Organ Culture

, Volume 38, Issue 2–3, pp 351–356 | Cite as

Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by wounding and methyl jasmonate

Implications for the production of anti-cancer alkaloids
  • Ignacio E. Maldonado-Mendoza
  • Ronald J. Burnett
  • Melina Lòpez-Meyer
  • Craig L. Nessler
Article

Abstract

HMGR (3-hydroxy-3-methylglutaryl-coenzyme A reductase; E.C.1.1.1.34) supplies mevalonate for the synthesis of many plant primary and secondary metabolites, including the terpenoid component of indole alkaloids. Suspension cultures of Camptotheca acuminata and Catharanthus roseus, two species valued for their anticancer indole alkaloids, were treated with the elicitation signal transducer methyl jasmonate (MeJA). RNA gel blot analysis from MeJA treated cultures showed a transient suppression of HMGR mRNA, followed by an induction in HMGR message. Leaf disks from transgenic tobacco plants containing a chimeric hmgl::GUS construct were also treated with MeJA and showed a dose dependent suppression of wound-inducible GUS activity. The suppression of the wound response by MeJA was limited to the first 4 h post-wounding, after which time MeJA application had no effect. The results are discussed in relation to the differential regulation of HMGR isogenes in higher plants.

Key words

Camptotheca acuminata Catharanthus roseus HMGR methyl jasmonate terpenoid indole alkaloids 

Abbreviations

GUS

β-glucuronidase

hmg

gene of hmgr

HMGR

3-hydroxy-3-methylglutaryl-coenzyme A reductase

JA

jasmonic acid

MeJA

methyl jasmonate

MUG

methylumbelliferyl-β-d-glucuronide

TDC

tryptophan decarboxylase

SDS

sodium dodecyl sulfate

SS

strictosidine synthase

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bevan M (1984) Binary Agrobacterium vectors for plant cell transformation. Nucl. Acids Res. 12: 8711–8721Google Scholar
  2. Bostock RM & Stermer BA (1989) Perspectives on wound healing in resistance to pathogens. Ann. Rev. Phytopathol. 27: 343–371Google Scholar
  3. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254Google Scholar
  4. Caelles C, Ferrer A, Bacells L, Hegardt FG & Boronat A (1989) Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxyl-3-methylglutaryl coenzyme A reductase. Plant Mol. Biol. 13: 627–638Google Scholar
  5. Choi D, Ward BL & Bostock RM (1992) Differential induction and suppression of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes in response to Phytophthora infestans and to its elicitor arachidonic acid. Plant Cell 4: 1333–1344Google Scholar
  6. Chye M-L, Tan C-T & Chua N-H (1992) Three genes encode 3-hydroxyl-3-methylglutary CoA reductase in Hevea brasiliensis: hmg1 and hmg3 are differentially expressed. Plant Mol. Biol. 19: 473–484Google Scholar
  7. Cordell GA (1974) The biosynthesis of indole alkaloids. Lloydia 37: 219–298Google Scholar
  8. De Luca V, Marineau C & Brisson N (1989) Molecular cloning and analysis of a cDNA encoding a plant tryptophan decarboxylase: comparison with animal dopa decarboxylases. Proc. Natl. Acad. Sci. USA 86: 2582–2586Google Scholar
  9. Eilert U, De Luca V, Constable F & Kurz WGW (1987) Elicitator-mediated induction of tryptophan decarboxylase and strictosidine synthase activities in cell suspension cultures of Catharanthus roseus. Arch. Biochem. Biophys. 254: 491–497Google Scholar
  10. Genschik P, Criqui M-C, Parmentier Y, Marbach J, Durr A, Fleck J & Jamet E (1992) Isolation and characterization of a cDNA encoding a 3-hydroxy-3-methylglutaryl coenzyme A reductase from Nicotiana sylvestris. Plant Mol. Biol. 20: 337–341Google Scholar
  11. Gundlach H, Müller MJ, Kutchan TM & Zenk MH (1992) Jasmonic acid is a signal transducer in elicitor-induced plant cell cultures. Proc. Natl. Acad. Sci. USA 89: 2389–2393Google Scholar
  12. Horsch RB, Fry JE, Hoffmann NL, Eichholtz D, Rogers SG & Fraley RT (1985) A simple and general method for transferring genes into plants. Science 227: 1229–1231Google Scholar
  13. Jefferson RA (1987) Assaying chimeric genes in plants: The GUS gene fusion system. Plant Mol. Biol. Rep. 5: 387–405Google Scholar
  14. Jefferson RA, Kavanagh TA & Bevan MW (1987) GUS fusions: β-Glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6: 3901–3907Google Scholar
  15. Jones JDG, Dunsmuir P & Bedbrook J (1985) High level expression of introduced chimeric genes in regenerated transformed plants. EMBO J. 4: 2411–2418Google Scholar
  16. Kutchan TM, Hampp N, Lottspeich F, Beyreuther K & Zenk MH (1988) The cDNA clone for strictosidine synthase from Rauvolfia serpentina. DNA sequence determination and expression in Escherichia coli. FEBS. Lett. 237: 40–44Google Scholar
  17. Learned RM & Fink GR (1989) 3-hydroxy-3-methylglutaryl coenzyme A reductase from Arabidopsis thaliana is structurally distinct from the yeast and animal enzyme. Proc. Natl. Acad. Sci. USA 86: 2779–2783Google Scholar
  18. Lückner M (1984) Secondary Metabolism in Microorganisms, Plants and Animals, Ed. 2. Springer-Verlag, New YorkGoogle Scholar
  19. Maldonado-Mendoza IE, Burnett RJ & Nessler CL (1992) Nucleotide sequence of a cDNA encoding a 3-hydroxy-3-methylglutaryl coenzyme A reductase from Catharanthus roseus. Plant Physiol. 100: 1613–1614Google Scholar
  20. McKnight TD, Rossner CA, Devagupta R, Scott AI & Nessler CL (1990) Nucleotide sequence of a cDNA encoding the vacuolar protein strictosidine synthase from Catharanthus roseus. Nucl. Acids Res. 16: 4939Google Scholar
  21. Merillon J-M, Doireau P, Guillot A, Chenieux J-C & Rideau M (1986) Indole alkaloid accumulation and tryptophan decarboxylase activity in Catharanthus roseus cells cultured in three different media. Plant Cell Rep. 5: 23–26Google Scholar
  22. Merillon J-M, Ouelhazi L, Doireau P, Chenieux J-C & Rideau M (1989) Metabolic changes and alkaloid production in habituated and non-habituated cells of Catharanthus roseus grown in hormone-free medium. Comparing hormone-deprived non-habituated cells with habituated cells. J. Plant Physiol. 134: 54–60Google Scholar
  23. Murashige T & Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol. Plant. 15: 473–497Google Scholar
  24. Narita JO & Gruissem W (1989) Tomato hydroxymethylglutaryl-CoA reductase is required early in fruit development but not during ripening. Plant Cell 1: 181–190Google Scholar
  25. Pasquali G, Goddijn OJM, de Waal A, Verpoorte R, Schilperoort RA, Hoge JHC & Memelink J (1992) Coordinated regulation of two indole alkaloid biosynthetic genes from Catharanthus roseus by auxin and elicitors. Plant Mol. Biol. 18: 1121–1131Google Scholar
  26. Roewer IA, Cloutier N, Nessler CL & De Luca V (1992) Transient induction of tryptophan decarboxylase (TDC) and strictosidine synthase (SS) genes in cell suspension culture of Catharanthus roseus. Plant Cell Rep. 11: 86–89Google Scholar
  27. Sakato K & Misawa M (1974) Effects of chemical and physical conditions on growth of Camptotheca acuminata cell cultures. Agric. Biol. Chem. 38: 491–49Google Scholar
  28. Stöckigt J & Zenk MH (1977) Isovincoside (strictosidine), the key intermediate in the enzymatic formation of indole alkaloids. FEBS Lett. 79: 233–237Google Scholar
  29. van Hengel AJ, Harkes MP, Wichers HJ, Hesselink PGM & Buitelaar RM (1992) Characterization of callus formation and camptothecin production by cell lines of Camptotheca acuminata. Plant Cell Tiss. Organ Cult. 28: 11–18Google Scholar
  30. Yang Z, Park H, Lacy GH & Cramer CL (1991) Differential activation of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes by wounding and pathogen challenge. Plant Cell 3: 397–405Google Scholar

Copyright information

© Kluwer Academic Publishers 1994

Authors and Affiliations

  • Ignacio E. Maldonado-Mendoza
    • 1
  • Ronald J. Burnett
    • 1
  • Melina Lòpez-Meyer
    • 1
  • Craig L. Nessler
    • 1
  1. 1.Department of BiologyTexas A&M UniversityCollege StationUSA

Personalised recommendations