Skip to main content
SpringerLink
Log in

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

Implications for the production of anti-cancer alkaloids

  • Published:
Plant Cell, Tissue and Organ Culture Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

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

References

  • Bevan M (1984) Binary Agrobacterium vectors for plant cell transformation. Nucl. Acids Res. 12: 8711–8721

    Google Scholar 

  • Bostock RM & Stermer BA (1989) Perspectives on wound healing in resistance to pathogens. Ann. Rev. Phytopathol. 27: 343–371

    Google Scholar 

  • 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: 248–254

    Google Scholar 

  • 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: 627–638

    Google Scholar 

  • 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: 1333–1344

    Google Scholar 

  • 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: 473–484

    Google Scholar 

  • Cordell GA (1974) The biosynthesis of indole alkaloids. Lloydia 37: 219–298

    Google Scholar 

  • 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: 2582–2586

    Google Scholar 

  • 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: 491–497

    Google Scholar 

  • 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: 337–341

    Google Scholar 

  • 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: 2389–2393

    Google Scholar 

  • 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: 1229–1231

    Google Scholar 

  • Jefferson RA (1987) Assaying chimeric genes in plants: The GUS gene fusion system. Plant Mol. Biol. Rep. 5: 387–405

    Google Scholar 

  • 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: 3901–3907

    Google Scholar 

  • Jones JDG, Dunsmuir P & Bedbrook J (1985) High level expression of introduced chimeric genes in regenerated transformed plants. EMBO J. 4: 2411–2418

    Google Scholar 

  • 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: 40–44

    Google Scholar 

  • 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: 2779–2783

    Google Scholar 

  • Lückner M (1984) Secondary Metabolism in Microorganisms, Plants and Animals, Ed. 2. Springer-Verlag, New York

    Google Scholar 

  • 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: 1613–1614

    Google Scholar 

  • 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: 4939

    Google Scholar 

  • 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: 23–26

    Google Scholar 

  • 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: 54–60

    Google Scholar 

  • Murashige T & Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol. Plant. 15: 473–497

    Google Scholar 

  • Narita JO & Gruissem W (1989) Tomato hydroxymethylglutaryl-CoA reductase is required early in fruit development but not during ripening. Plant Cell 1: 181–190

    Google Scholar 

  • 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: 1121–1131

    Google Scholar 

  • 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: 86–89

    Google Scholar 

  • Sakato K & Misawa M (1974) Effects of chemical and physical conditions on growth of Camptotheca acuminata cell cultures. Agric. Biol. Chem. 38: 491–49

    Google Scholar 

  • Stöckigt J & Zenk MH (1977) Isovincoside (strictosidine), the key intermediate in the enzymatic formation of indole alkaloids. FEBS Lett. 79: 233–237

    Google Scholar 

  • 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: 11–18

    Google Scholar 

  • 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: 397–405

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biology, Texas A&M University, 77843-3258, College Station, Texas, USA

    Ignacio E. Maldonado-Mendoza, Ronald J. Burnett, Melina Lòpez-Meyer & Craig L. Nessler

Authors
  1. Ignacio E. Maldonado-Mendoza
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ronald J. Burnett
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Melina Lòpez-Meyer
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Craig L. Nessler
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Maldonado-Mendoza, I.E., Burnett, R.J., Lòpez-Meyer, M. et al. Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by wounding and methyl jasmonate. Plant Cell Tiss Organ Cult 38, 351–356 (1994). https://doi.org/10.1007/BF00033896

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00033896

Key words

Search

Navigation