Application of carborundum abrasion for investigating the leaf epidermis: Molecular cloning of Catharanthus roseus 16-hydroxytabersonine-16-O- methyltransferase

Plant Journal

Volumn 53, Issue 2, 2008, Pages 225-236

  Levac, Dylan ^c   Murata, Jun ^a,c   Kim, Won S ^b,c   De Luca, Vincenzo ^c  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b AGRICULTURE AND AGRI FOOD CANADA   (Canada)

^c BROCK UNIVERSITY   (Canada)

Author keywords

16 hydroxytabersonine 16 O methyltransferase (16OMT); Carborundum abrasion; Catharanthus roseus (Madagascar periwinkle); Cellular localization; Enrichment of leaf epidermal proteins and mRNA; Gene expression

Indexed keywords

CARBORUNDUM ABRASION; CATHARANTHUS ROSEUS; CELLULAR LOCALIZATION; ENRICHMENT OF LEAF EPIDERMAL PROTEINS;

ABRASION; BIOCHEMISTRY; ENZYMES; GENE EXPRESSION; SUBSTRATES;

CLONING;

16 METHOXYTABERSONINE METHYLTRANSFERASE, CATHARANTHUS ROSEUS; 16-METHOXYTABERSONINE METHYLTRANSFERASE, CATHARANTHUS ROSEUS; CATHARANTHINE; DRUG DERIVATIVE; INDOLE ALKALOID; METHYLTRANSFERASE; QUINOLINE DERIVATIVE; RECOMBINANT PROTEIN; TABERSONINE; UNCLASSIFIED DRUG; VINBLASTINE; VINCA ALKALOID; VINDOLINE;

ARTICLE; CATHARANTHUS; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PLANT EPIDERMIS; PLANT LEAF;

CATHARANTHUS; CLONING, MOLECULAR; INDOLE ALKALOIDS; KINETICS; METHYLTRANSFERASES; MOLECULAR SEQUENCE DATA; PLANT EPIDERMIS; PLANT LEAVES; QUINOLINES; RECOMBINANT PROTEINS; VINBLASTINE; VINCA ALKALOIDS;

CATHARANTHUS; CATHARANTHUS ROSEUS;

EID: 37749042422     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2007.03337.x     Document Type: Article

References (31)

1. Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, Z., Miller, W. Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389 3402.
2. Cacacea, S., Schröder, G., Wehingera, E., Strack, D., Schmidt, J. Schröder, J. (2003) A flavonol O-methyltransferase from Catharanthus roseus. Phytochemistry, 62, 127 137.
3. Choi, Y.H., Yoo, K.P. Kim, J. (2002) Supercritical fluid extraction and liquid chromatography-electrospray. Chem. Pharm. Bull. 50, 1294 1296.
4. De Luca, V. Cutler, A.J. (1987) Subcellular localization of enzymes involved in indole alkaloid biosynthesis in Catharanthus roseus. Plant Physiol. 85, 1099 1102.
5. De Luca, V., Balsevich, J., Tyler, R.T. Kurz, W.G.W. (1987) Characterization of a novel N-methyltransferase (NMT) from Catharanthus roseus plants. Detection of NMT and other enzymes of the indole alkaloid biosynthetic pathway in different cell suspension culture systems. Plant Cell Rep. 6, 458 461.
6. De Luca, V., Alvarez Fernandez, J.A., Campbell, D. Kurz, W. (1988) Developmental regulation of enzymes of indole alkaloid biosynthesis in Catharanthus roseus. Plant Physiol. 86, 447 450.
7. Dethier, M. De Luca, V. (1993) Partial purification of an N-methyltransferase involved in vindoline biosynthesis in Catharanthus roseus. Phytochemistry, 32, 673 678.
8. Fahn, W., Laussermair, E., Deus-Neumann, B. Stöckigt, J. (1985) Late enzymes of vindoline biosynthesis. S-adenosyl-l-methionine:11-O-demethyl-17-O- deacetylvindoline 11-O-methyltransferase and unspecific acetylesterase. Plant Cell Rep. 4, 337 340.
9. Fahy, J., Duflos, A., Ribet, J.P., Jaequesy, J.C., Berrier, C., Jonannetaud, M.P. Zonino, F.D. (1997) Vinca alkaloids in superacidic media: a method for creating a new family of antitumor. J. Am. Chem. Soc. 119, 8576 8577.
10. Fridman, E., Wang, J., Iijima, Y., Froehlich, J.E., Gang, D.R., Ohlrogge, J. Pichersky, E. (2005) Metabolic, genomic, and biochemical analyses of glandular trichomes from the wild tomato species Lycopersicon hirsutum identify a key enzyme in the biosynthesis of methylketones. Plant Cell, 17, 1252 1267.
11. Gang, D.R., Wang, J., Dudareva, N., Nam, K.H., Simon, J.E., Lewinsohn, E. Pichersky, E. (2001) An investigation of the storage and biosynthesis of phenylpropenes in sweet basil. Plant Physiol. 125, 539 555.
12. James, F., Nolte, K.D. Hanson, A.D. (1995) Purification and properties of S-adenosyl-l-methionine:l-methionine S-methyltransferase from Wollastonia biflora leaves. J. Biol. Chem. 270, 22 344 22350.
13. Kopito, R. (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524 530.
14. Koch, M., Lemke, R., Heise, K.P. Mock, H.P. (2003) Characterization of c-tocopherol methyltransferases from Capsicum annuum L. and Arabidopsis thaliana. Eur. J. Biochem. 270, 84 92.
15. Lange, B.M., Wildung, M.R., Stauber, E.J., Sanchez, C., Pouchnik, D. Croteau, R. (2000) Probing essential oil biosynthesis and secretion by functional evaluation of expressed sequence tags from mint glandular trichomes. Proc. Natl Acad. Sci. U.S.A. 97, 2934 2939.
16. Lin, F., Yamano, G., Hasegawa, M. Anzai, H. (2006) Cloning and functional analysis of caffeic acid 3-O-methyltransferase from rice (Oryza sativa). J. Pesticide Sci. 31, 47 53.
17. Moreno, P., van der Heijden, R. Verpoorte, R. (1995) Cell and tissue cultures of Catharanthus roseus: a literature survey. Plant Cell Tissue Organ Cult. 42, 1 25.
18. Murata, J. De Luca, V. (2005) Localization of tabersonine 16-hydroxylase and 16-hydroxytabersonine-16-O-methyltransferase to leaf epidermal cells defines them as a major site of precursor biosynthesis in the vindoline pathway in Catharanthus roseus. Plant J. 44, 581 594.
19. Murata, J., Bienzle, D., Brandle, J.E., Sensen, C.W. De Luca, V. (2006) Expressed sequence tags from Madagascar periwinkle (Catharanthus roseus). FEBS Lett. 580, 4501 4507.
20. Nakazono, M., Qiu, F., Borsuk, L.A. Schnable, P.S. (2003) Laser-capture microdissection, a tool for the global analysis of gene expression in specific plant cell types: identification of genes expressed differentially in epidermal cells or vascular tissues of maize. Plant Cell, 15, 583 596. Erratum in Plant Cell (2003) 15, 1049.
21. Schröder, G., Unterbusch, E., Kaltenbach, M., Schmidt, J., Strack, D., De Luca, V. Schröder, J. (1999) Light-induced cytochrome P450-dependent enzyme in indole alkaloid biosynthesis: tabersonine 16-hydroxylase. FEBS Lett. 458, 97 102.
22. Schröder, G., Wehinger, E. Schröder, J. (2002) Predicting the substrates of cloned plant O-methyltransferases. Phytochemistry, 59, 1 8.
23. Schröder, G., Wehinger, E., Lukačin, R., Wellmann, F., Seefelder, W., Schwab, W. Schröder, J. (2004) Flavonoid methylation: a novel 4′-O-methyltransferase from Catharanthus roseus, and evidence that partially methylated flavanones are substrates of four different flavonoid dioxygenases. Phytochemistry, 65, 1085 1094.
24. Schubert, H., Blumenthal, R. Cheng, X. (2003) Many paths to methyltransfer: a chronicle of convergence. Trends Biochem. Sci. 28, 329 335.
25. St Pierre, B., Laflamme, P., Alarco, A.M. De Luca, V. (1998) The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer. Plant J. 14, 703 713.
26. St Pierre, B., Vazquez-Flota, F. De Luca., V. (1999) Multicellular compartmentation of alkaloid biosynthesis predicts intercellular translocation of a pathway intermediate. Plant Cell, 11, 887 900.
27. Tikhomiroff, C. Jolicoeur, M. (2002) Screening of Catharanthus roseus secondary metabolites by high-performance liquid chromatography. J. Chromatogr. A. 955, 87 93.
28. Vázquez-Flota, F.A., Moreno-Valenzuela, O., Miranda-Ham, M.L., Coello-Coello, J. Loyola-Vargas, V.M. (1994) Catharanthine and ajmalicine synthesis in Catharanthus roseus hairy root cultures. Plant Cell Tissue Organ Cult. 38, 273 279.
29. Vázquez -Flota, F.A. De Luca, V. (1998) Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in Catharanthus roseus (L.) G. Don. Evidence of a multilevel regulatory mechanism. Plant Physiol. 117, 1351 1361.
30. Wagner, G.J., Wang, E. Shepherd, R. W. (2004) New approaches for studying and exploiting an old protuberance, the plant trichome. Ann. Bot. 93, 3 11.
31. Zubieta, C., He, X.Z., Dixon, R.A. Noel, J.P. (2001) Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat. Struct. Biol. 8, 271 279.