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. 1995 Oct;109(2):717–720. doi: 10.1104/pp.109.2.717

Tryptophan Decarboxylase, Tryptamine, and Reproduction of the Whitefly.

J C Thomas 1, D G Adams 1, C L Nessler 1, J K Brown 1, H J Bohnert 1
PMCID: PMC157640  PMID: 12228625

Abstract

Tryptophan decarboxylase (TDC) from Catharanthus roseus (periwinkle) converts tryptophan to the indole-alkaloid tryptamine. When the TDC gene was expressed in transgenic tobacco, the 55-kD TDC enzyme and tryptamine accumulated. Bemisia tabaci (sweetpotato whitefly) reproduction on transgenic plants decreased up to 97% relative to controls. Production of tryptamine, its derivatives, or other products resulting from TDC activity may discourage whitefly reproduction and provide a single-gene-based plant protection strategy.

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Selected References

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  1. A simple and general method for transferring genes into plants. Science. 1985 Mar 8;227(4691):1229–1231. doi: 10.1126/science.227.4691.1229. [DOI] [PubMed] [Google Scholar]
  2. Benfey P. N., Ren L., Chua N. H. Tissue-specific expression from CaMV 35S enhancer subdomains in early stages of plant development. EMBO J. 1990 Jun;9(6):1677–1684. doi: 10.1002/j.1460-2075.1990.tb08291.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bracher D., Kutchan T. M. Strictosidine synthase from Rauvolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis. Arch Biochem Biophys. 1992 May 1;294(2):717–723. doi: 10.1016/0003-9861(92)90746-j. [DOI] [PubMed] [Google Scholar]
  4. Csaba G. Presence in and effects of pineal indoleamines at very low level of phylogeny. Experientia. 1993 Aug 15;49(8):627–634. doi: 10.1007/BF01923943. [DOI] [PubMed] [Google Scholar]
  5. De Luca V., Fernandez J. A., Campbell D., Kurz W. G. Developmental Regulation of Enzymes of Indole Alkaloid Biosynthesis in Catharanthus roseus. Plant Physiol. 1988 Feb;86(2):447–450. doi: 10.1104/pp.86.2.447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ghosh S., Gepstein S., Heikkila J. J., Dumbroff E. B. Use of a scanning densitometer or an ELISA plate reader for measurement of nanogram amounts of protein in crude extracts from biological tissues. Anal Biochem. 1988 Mar;169(2):227–233. doi: 10.1016/0003-2697(88)90278-3. [DOI] [PubMed] [Google Scholar]
  7. Jefferson R. A., Kavanagh T. A., Bevan M. W. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 1987 Dec 20;6(13):3901–3907. doi: 10.1002/j.1460-2075.1987.tb02730.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Johnson R., Narvaez J., An G., Ryan C. Expression of proteinase inhibitors I and II in transgenic tobacco plants: effects on natural defense against Manduca sexta larvae. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9871–9875. doi: 10.1073/pnas.86.24.9871. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. King R. W., Zeevaart J. A. Enhancement of Phloem exudation from cut petioles by chelating agents. Plant Physiol. 1974 Jan;53(1):96–103. doi: 10.1104/pp.53.1.96. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Perlak F. J., Deaton R. W., Armstrong T. A., Fuchs R. L., Sims S. R., Greenplate J. T., Fischhoff D. A. Insect resistant cotton plants. Biotechnology (N Y) 1990 Oct;8(10):939–943. doi: 10.1038/nbt1090-939. [DOI] [PubMed] [Google Scholar]

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