Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 67, 2003 - Issue 5
Journal homepage
247
Views
11
CrossRef citations to date
0
Altmetric
Original Articles

Induction Mechanism of 3-Hydroxy-3-methylglutaryl-CoA Reductase in Potato Tuber and Sweet Potato Root Tissues

Katsuyoshi KONDOLaboratory of Food Biochemistry, Nagoya Women's University3-40 Shioji, Mizuho, Nagoya 467-8610, Japan;Present address: Takemoto Oil & Fat Co.,Ltd.2-5 Minato-machi, Gamagori, Aichi 443-8611, Japan
,
Ikuzo URITANILaboratory of Food Biochemistry, Nagoya Women's University3-40 Shioji, Mizuho, Nagoya 467-8610, Japan
&
Kazuko OBALaboratory of Food Biochemistry, Nagoya Women's University3-40 Shioji, Mizuho, Nagoya 467-8610, Japan
Pages 1007-1017 | Received 30 Oct 2002, Accepted 15 Jan 2003, Published online: 22 May 2014

  • 1) Lange, B. M., Rujan, T., Martin, W., and Croteau, R., Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes. Proc. Natl. Acad. Sci. USA, 97, 13172-13177 (2000).
  • 2) Schwender, J., Seemann, M., Lichtenthaler, H. K., and Rohmer, M., Biosynthesis of isoprenoids (catotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via novel pyruvate/glyceraldehydes 3-phosphate nonmevalonate pathway in the green alga Scenedesmus obliquus. Biochem. J., 316, 73-80 (1996).
  • 3) Newman, J. D., and Chappell, J., Isoprenoid biosynthesis in plants: carbon partitioning within the cytoplasmic pathway. Crit. Rev. Biochem. Mol. Biol., 34, 95-106 (1997).
  • 4) Bach, T. J., Synthesis and metabolism of mevalonic acid in plnats. Plant Physiol. Biochem., 25, 163-178 (1987).
  • 5) Chappell, J., Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol., 46, 521-547 (1995).
  • 6) Brown, M. S., and Goldstein, J. L., Regulation of the mevalonate pathway. Nature, 343, 425-430 (1990).
  • 7) Oba, K., Kondo, K., Doke, N., and Uritani, I., Induction of 3-hydroxy-3-methylglutaryl CoA reductase in potato tubers after cutting, fungal infection or chemical treatment and some properties of the enzyme. Plant Cell Physiol., 26, 873-880 (1985).
  • 8) Suzuki, H., Oba, K., and Uritani, I., The occurrence and some properties of 3-hydroxy-3methylgluraryl coenzyme A reductase in sweet potato roots infected by Ceratocystis fimbriata. Physiol. Plant Patholo., 7, 265-276 (1975).
  • 9) Oba, K., Oga, K., and Uritani, I., Metabolism of Ipomeamarone in sweet potato root slices before and after treatment with mercuric chloride or infection with Ceratocystis fimbriata. Phytochemistry, 21, 1921-1925 (1982).
  • 10) Ito, R., Oba, K., and Uritani, I., Mechanism for the induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase in HgCl2-treated sweet potato root tissue. Plant Cell Physiol., 20, 867-874 (1979).
  • 11) Jelesko, J. G., Jenkins, S. M., Rodriguez-Concepcion, M., and Gruissem, W., Regulation of tomato hmg1 during cell proliferation and growth. Planta, 208, 310-318 (1999).
  • 12) Godoy-Hernandez, G. C., Chappell, J., Devarenne, T. P., Garcia-Pineda, E., Guevara-Garcia, A. A., and Lozoya-Gloria, E., Antisense expression of hmg1 from Arabidopsis thaliana encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase reduces isoprenoid production in transgenic tobacco plants. J. Plant Physiol., 153, 415-424 (1998).
  • 13) Bhattacharyya, M. K., Paiva, N. L., Dixon, R. A., Korth, K. L., and Stermer, B. A., Features of the hmg1 subfamily of genes encoding HMG-CoA reductase in potato. Plant Mol. Biol., 28, 1-15 (1995).
  • 14) Yang, Z., Park, H., Lacy, G. H., and Cramer, C. L., Differential activation of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes by wounding and pathogen challenge. Plant Cell, 3, 397-405 (1991).
  • 15) Burnett, R. J., Maldonado-Mendoza, I. E., McKnight, T. D., and Nessler, C. L., Expression of a 3-hydroxy-3-methylglutaryl coenzyme A reductase gene from Camptotheca acuminata is differentially regulated by wounding and methyl jasmonate. Plant Physiol., 103, 41-48 (1993).
  • 16) Yoshioka, H., Miyabe, M., Hayakawa, Y., and Doke, N., Expression of genes for phenylalanine ammonia-lyase and 3-hydroxy-3-methylglutaryl CoA reductase in aged potato tubers infected with Phytophthora infestans. Plant Cell Physiol., 37, 81-90 (1996).
  • 17) Caelles, C., Ferrer, A., Balcells, L., Hegardt, F. G., and Boronat, A., Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Mol. Biol., 13, 627-638 (1989).
  • 18) Genschik, P., Criqui, M.-C., Parmentier, Y., Marbach, J., Durr, A., Fleck, J., and Jamet, E., Isolation and characterization of a cDNA encoding a 3-hydroxy-3-methylglutaryl coenzyme A reductase from Nicotiana sylvestris. Plant Mol. Biol., 20, 337-341 (1992).
  • 19) Choi, D., Ward, B. L., and Bostock, R. M., 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 (1992).
  • 20) Korth, K. L., Stermer, B. A., Bhattacharyya, M. K., and Dixon, R. A., HMG-CoA reductase gene families that differentially accumulate transcripts in potato tubers are developmentally expressed in floral tissue. Plant Mol. Biol., 33, 545-551 (1997).
  • 21) Chye, M.-L., Tan, C.-T., and Chua, N.-H., Three genes encode 3-hydroxy-3-methylglutaryl coenzyme A reductase in Hevea brasiliensis: hmg1 and hmg3 are differentially expressed. Plant Mol. Biol., 19, 473-484 (1992).
  • 22) Park, H., Denbow, C. J., and Cramer, C. L., Structure and nucleotide sequence of tomato hmg2 encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Mol. Biol., 20, 327-331 (1992).
  • 23) Loguercio, L. L., Scott, H. C., Trolinder, N. L., and Wilkins, T. A., HMG-CoA reductase gene family in cotton (Gossypium hirsutum L.): unique structural features and differential expression of hmg2 potentially associated with synthesis of specific isoprenoids in developing embryos. Plant Cell Physiol., 40, 750-761 (1999).
  • 24) Aoyagi, K., Beyou, A., Moon, K., Fang, L., and Ulrich, T., Isolation and characterization of cDNAs encoding wheat 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Physiol., 102, 623-628 (1993).
  • 25) Kondo, K., and Oba, K., Purification and characterization of 3-hydroxy-3-methylglutaryl CoA reductase from potato tubers. J. Biochem., 100, 967-974 (1986).
  • 26) Doke, N., and Tomiyama, K., Effect of hyphal wall components from Phytophthora infestans on protoplasts of potato tuber tissues. Physiol. Plant Pathol., 16, 169-176 (1980).
  • 27) Shapiro, D. J., Imblum, R. L., and Rodwell, V. W., Thinlayer chromatographic assay for HMG-CoA reductase and mevalonic acid. Anal. Biochem., 31, 383-390 (1969).
  • 28) Yu-Ito, R., Oba, K., and Uritani, I., Some problems in the assay method of HMG-CoA reductase activity in sweet potato in the presence of other HMG-CoA utilizing enzymes. Agric. Biol. Chem., 46, 2087-2091 (1982).
  • 29) Hämmerling, G. J., Lemke, H., Hämmerling, U., Höhmann, C., Wallich, R., and Rajewsky, K., Monoclonal antibodies against murine cell surface antigens: Anti-H-2, Anti-Ia and Anti-T cell antibodies. Curr. Top. Microbiol. Immunol., 81, 100-106 (1978).
  • 30) McConahey, P. J., and Dixon, F. J., A method of trace iodination of proteins for immunologic studies. Int. Arch. Allergy, 29, 185-189 (1966).
  • 31) Laemmili, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
  • 32) Towbin, H., Staehelin, T., and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA, 76, 4350-4354 (1979).
  • 33) Harlow, E., and Lane, D. C., Antibodies:A laboratory manual, Cold Spring Harbor, Cold Spring Harbor Laboratory Press, P. 471-510 (1988).
  • 34) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-268 (1951).
  • 35) Ouchterlony, O., and Nilsson, L. A., Immunodiffusion and immunoelectrophoresis. In “Handbook of Experimental Immunology”, ed. Weir, D. M., Blackwell Scientific Publications, Oxford, P. 19.1-19.39 (1973).
  • 36) Korth, K. L., Jaggard, D. A. W., and Dixon, R. H., Developmental and light-regulated post-translational control of 3-hydroxy-3-methylglutaryl-CoA reductase levels in potato. Plant J., 23, 507-516 (2000).
  • 37) Kobayashi, T., Kato-Emori, S., Tomita, K., and Ezura, H., Detection of 3-hydroxy-3-methylglutaryl-coenzyme A reductase protein Cm-HMGR during fruit development in melon (Cucumis melo L.). Theor. Appl. Genet., 104, 779-785 (2002).
  • 38) Ishizaki, N., and Tomiyama, K., Effect of wounding or infection by Phytophthora infestans on the contents of terpenoids in potato tubers. Plant Cell Physiol., 13, 1053-1063 (1972).
  • 39) Allen, E. H., and Kuc, J., α-Solanin and α-chaconine as fungitoxic compounds in extracts of Irish potato tubers. Phytopathology, 58, 776-781 (1968).
  • 40) Kuc, J., Currier, W. W., and Shih, M. J., Terpenoid phytoalexin. In “Biochemical Aspects of Plant-Parasite Relationship”, eds. Friend, J., and Threfall, D. R., Academic Press, London, pp. 225-237 (1976).
  • 41) Vollack, K. U., Dittrich, B., Ferrer, A., Boronat, A., and Bach, T. J., Two radish genes for 3-hydroxy-3-methylglutaryl-CoA reductase isozymes complement mevalonate autotrophy in a yeast mutant and yield membrane-bound active enzyme. J. Plant Physiol., 143, 479-487 (1994).
  • 42) Hemmerlin, A., and Bach, T. J., Effect of mevinolin on cell cycle progression and viability of tobacco BY-2 cells. Plant J., 14, 65-74 (1998).
  • 43) Choi, D., Bostock, R. M., Avdiushko, S., and Hildebrand, D. F., Lipid-derived signals that discriminate wound- and pathogen-responsive isoprenoid pathways in plants: methyl jasmonate and the fungal elicitor arrachidonic acid induce different 3-hydroxy-3-methylglutaryl-coenzyme A reductase genes and antimicrobial isoprenoids in Solanum tuberosum L. Proc. Natl. Acad. Sci. USA, 91, 2329-2333 (1994).
  • 44) Muranaka, T., Regulation of the mevalonate pathway. Chemical Regulation of Plant (in Japanese), 32, 150-159 (1997).
  • 45) Toroser, D., and Huber, S. C., 3-Hydroxy-3-methylglutaryl-coenzyme A reductase kinase and sucrose-phosphate synthase kinase activities in cauliflower florets: Ca2+ dependence and substrate specificities. Arch. Biochem. Biophys., 355, 291-300 (1998).
  • 46) Douglas, P., Pigaglio, E., Ferrer, A., Halford, N. G., and MacKintosh, C., Three spinach leaf nitrate reductase and 3-hydroxy-3-methylglutaryl CoA reductase kinases that are regulated by reversible phosphorylation and/or Ca2+ ions. Biochem. J., 325, 101-109 (1997).
  • 47) Sugden, C., Donaghy, P. G., Halford, N. G., and Hardie, D. G., Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro. Plant Physiol., 120, 257-274 (1999).
  • 48) Yoshida, S., and Muranaka, T., Approaches to unique technologies for regulation of plant growth functions. Nippon Nogeikagaku Kaishi (in Japanese), 76, 37-41 (2002).
  • 49) Dale, S., Arro, M. B., Morrice, N. G., Boronat, A., Hardie, D. G., and Ferrer, A., Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana. and its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-hydroxy-3-methylglutaryl-CoA reductase kinase. Eur. J. Biochem., 233, 506-513 (1995).
  • 50) Mackintosh, R. W., Davies, S. P., Clarke, P. R., Weekes, J., Gillespie, J. G., Gibb, B. J., and Hardie, D. G., Evidence for a protein kinase cascade in higher plants: 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase. Eur. J. Biochem., 209, 923-931 (1992).
  • 51) Parker, R. A., Miller, S. J., and Gibson, D. M., Phosphorylation of microsomal HMG-CoA reductase increases susceptibility to proteolytic degradation in vitro. Biochem. Biophys. Res. Commun., 125, 629-635 (1984).
  • 52) Stermer, B. A., Bianchini, G. M., and Korth, K. L., Regulation of HMG-CoA reductase activity in plants. J. Lipid Res., 35, 1133-1140 (1994).
  • 53) Oosterhaven, K., Hartmans, K. J., and Huizing, H. J., Inhibition of potato (Solanum tuberosum) sprout growth by the monoterpene S-carvone: reduction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity without effect on its mRNA level. J. Plant Physiol., 141, 463-469 (1993).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.