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. 1995 Aug;108(4):1413–1421. doi: 10.1104/pp.108.4.1413

Impaired Wound Induction of 3-Deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) Synthase and Altered Stem Development in Transgenic Potato Plants Expressing a DAHP Synthase Antisense Construct.

J D Jones 1, J M Henstrand 1, A K Handa 1, K M Herrmann 1, S C Weller 1
PMCID: PMC157519  PMID: 12228551

Abstract

Potato (Solanum tuberosum L.) cells were transformed with an antisense DNA construct encoding part of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthase (EC 4.1.2.15), the first enzyme of the shikimate pathway, to examine the role(s) of this protein in plant growth and development. Chimeric DNA constructs contained the transcript start site, the first exon, and part of the first intron of the shkA gene in antisense or sense orientations under the control of the cauliflower mosaic virus 35S promoter. Some, but not all, of the transgenic plants expressing antisense DAHP synthase RNA showed reduced levels of wound-induced DAHP synthase enzyme activity, polypeptide, and mRNA 12 and 24 h after wounding. No alteration in the wound induction of DAHP synthase gene expression was observed in transgenic potato tubers containing the chimeric sense construct. Reduced steady-state levels of DAHP synthase mRNA were observed in stem and shoot tip tissue. Some plants with the chimeric antisense construct had reduced stem length, stem diameter, and reduced stem lignification.

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Selected References

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  1. Beaudoin-Eagan L. D., Thorpe T. A. Shikimate Pathway Activity during Shoot Initiation in Tobacco Callus Cultures. Plant Physiol. 1983 Oct;73(2):228–232. doi: 10.1104/pp.73.2.228. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Beck E., Ludwig G., Auerswald E. A., Reiss B., Schaller H. Nucleotide sequence and exact localization of the neomycin phosphotransferase gene from transposon Tn5. Gene. 1982 Oct;19(3):327–336. doi: 10.1016/0378-1119(82)90023-3. [DOI] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  4. Bruce R. J., West C. A. Elicitation of lignin biosynthesis and isoperoxidase activity by pectic fragments in suspension cultures of castor bean. Plant Physiol. 1989 Nov;91(3):889–897. doi: 10.1104/pp.91.3.889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Elkind Y., Edwards R., Mavandad M., Hedrick S. A., Ribak O., Dixon R. A., Lamb C. J. Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene. Proc Natl Acad Sci U S A. 1990 Nov;87(22):9057–9061. doi: 10.1073/pnas.87.22.9057. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Goldsbrough P. B., Cullis C. A. Characterisation of the genes for ribosomal RNA in flax. Nucleic Acids Res. 1981 Mar 25;9(6):1301–1309. doi: 10.1093/nar/9.6.1301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Görlach J., Beck A., Henstrand J. M., Handa A. K., Herrmann K. M., Schmid J., Amrhein N. Differential expression of tomato (Lycopersicon esculentum L.) genes encoding shikimate pathway isoenzymes. I. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Plant Mol Biol. 1993 Nov;23(4):697–706. doi: 10.1007/BF00021525. [DOI] [PubMed] [Google Scholar]
  8. Görlach J., Schmid J., Amrhein N. Abundance of transcripts specific for genes encoding enzymes of the prechorismate pathway in different organs of tomato (Lycopersicon esculentum L.) plants. Planta. 1994;193(2):216–223. doi: 10.1007/BF00192533. [DOI] [PubMed] [Google Scholar]
  9. Henstrand J. M., McCue K. F., Brink K., Handa A. K., Herrmann K. M., Conn E. E. Light and Fungal Elicitor Induce 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthase mRNA in Suspension Cultured Cells of Parsley (Petroselinum crispum L.). Plant Physiol. 1992 Feb;98(2):761–763. doi: 10.1104/pp.98.2.761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jones J. D., Weller S. C., Goldsbrough P. B. Selection for kanamycin resistance in transformed petunia cells leads to the co-amplification of a linked gene. Plant Mol Biol. 1994 Feb;24(3):505–514. doi: 10.1007/BF00024118. [DOI] [PubMed] [Google Scholar]
  11. Keith B., Dong X. N., Ausubel F. M., Fink G. R. Differential induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase genes in Arabidopsis thaliana by wounding and pathogenic attack. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8821–8825. doi: 10.1073/pnas.88.19.8821. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kuipers AGJ., Jacobsen E., Visser RGF. Formation and Deposition of Amylose in the Potato Tuber Starch Granule Are Affected by the Reduction of Granule-Bound Starch Synthase Gene Expression. Plant Cell. 1994 Jan;6(1):43–52. doi: 10.1105/tpc.6.1.43. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. McCue K. F., Conn E. E. Induction of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase activity by fungal elicitor in cultures of Petroselinum crispum. Proc Natl Acad Sci U S A. 1989 Oct;86(19):7374–7377. doi: 10.1073/pnas.86.19.7374. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Muday G. K., Herrmann K. M. Wounding Induces One of Two Isoenzymes of 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthase in Solanum tuberosum L. Plant Physiol. 1992 Feb;98(2):496–500. doi: 10.1104/pp.98.2.496. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Muday G. K., Johnson D. I., Somerville R. L., Herrmann K. M. The tyrosine repressor negatively regulates aroH expression in Escherichia coli. J Bacteriol. 1991 Jun;173(12):3930–3932. doi: 10.1128/jb.173.12.3930-3932.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ogino T., Garner C., Markley J. L., Herrmann K. M. Biosynthesis of aromatic compounds: 13C NMR spectroscopy of whole Escherichia coli cells. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5828–5832. doi: 10.1073/pnas.79.19.5828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Oliver M. J., Ferguson D. L., Burke J. J., Velten J. Inhibition of tobacco NADH-hydroxypyruvate reductase by expression of a heterologous antisense RNA derived from a cucumber cDNA: implications for the mechanism of action of antisense RNAs. Mol Gen Genet. 1993 Jun;239(3):425–434. doi: 10.1007/BF00276941. [DOI] [PubMed] [Google Scholar]
  18. Ooms G., Hooykaas P. J., Moolenaar G., Schilperoort R. A. Grown gall plant tumors of abnormal morphology, induced by Agrobacterium tumefaciens carrying mutated octopine Ti plasmids; analysis of T-DNA functions. Gene. 1981 Jun-Jul;14(1-2):33–50. doi: 10.1016/0378-1119(81)90146-3. [DOI] [PubMed] [Google Scholar]
  19. Palomares R., Herrmann R. G., Oelmuller R. Antisense RNA for components associated with the oxygen-evolving complex and the Rieske iron/sulfur protein of the tobacco thylakoid membrane suppresses accumulation of mRNA, but not of protein. Planta. 1993;190(3):305–312. doi: 10.1007/BF00196958. [DOI] [PubMed] [Google Scholar]
  20. Pinto J. E., Dyer W. E., Weller S. C., Herrmann K. M. Glyphosate Induces 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthase in Potato (Solanum tuberosum L.) Cells Grown in Suspension Culture. Plant Physiol. 1988 Aug;87(4):891–893. doi: 10.1104/pp.87.4.891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pinto J. E., Suzich J. A., Herrmann K. M. 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthase from Potato Tuber (Solanum tuberosum L.). Plant Physiol. 1986 Dec;82(4):1040–1044. doi: 10.1104/pp.82.4.1040. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schardl C. L., Byrd A. D., Benzion G., Altschuler M. A., Hildebrand D. F., Hunt A. G. Design and construction of a versatile system for the expression of foreign genes in plants. Gene. 1987;61(1):1–11. doi: 10.1016/0378-1119(87)90359-3. [DOI] [PubMed] [Google Scholar]
  23. Schoner R., Herrmann K. M. 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli. J Biol Chem. 1976 Sep 25;251(18):5440–5447. [PubMed] [Google Scholar]
  24. Suzich J. A., Ranjeva R., Hasegawa P. M., Herrmann K. M. Regulation of the shikimate pathway of carrot cells in suspension culture. Plant Physiol. 1984 Jun;75(2):369–371. doi: 10.1104/pp.75.2.369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Temple S. J., Knight T. J., Unkefer P. J., Sengupta-Gopalan C. Modulation of glutamine synthetase gene expression in tobacco by the introduction of an alfalfa glutamine synthetase gene in sense and antisense orientation: molecular and biochemical analysis. Mol Gen Genet. 1993 Jan;236(2-3):315–325. doi: 10.1007/BF00277128. [DOI] [PubMed] [Google Scholar]
  26. Tieman D. M., Harriman R. W., Ramamohan G., Handa A. K. An Antisense Pectin Methylesterase Gene Alters Pectin Chemistry and Soluble Solids in Tomato Fruit. Plant Cell. 1992 Jun;4(6):667–679. doi: 10.1105/tpc.4.6.667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Visser R. G., Somhorst I., Kuipers G. J., Ruys N. J., Feenstra W. J., Jacobsen E. Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs. Mol Gen Genet. 1991 Feb;225(2):289–296. doi: 10.1007/BF00269861. [DOI] [PubMed] [Google Scholar]
  28. Zhao J., Herrmann K. M. Cloning and Sequencing of a Second cDNA Encoding 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthase from Solanum tuberosum L. Plant Physiol. 1992 Oct;100(2):1075–1076. doi: 10.1104/pp.100.2.1075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Zrenner R., Willmitzer L., Sonnewald U. Analysis of the expression of potato uridinediphosphate-glucose pyrophosphorylase and its inhibition by antisense RNA. Planta. 1993;190(2):247–252. doi: 10.1007/BF00196618. [DOI] [PubMed] [Google Scholar]
  30. van der Krol A. R., Mol J. N., Stuitje A. R. Modulation of eukaryotic gene expression by complementary RNA or DNA sequences. Biotechniques. 1988 Nov-Dec;6(10):958–976. [PubMed] [Google Scholar]
  31. van der Krol A. R., Mur L. A., Beld M., Mol J. N., Stuitje A. R. Flavonoid genes in petunia: addition of a limited number of gene copies may lead to a suppression of gene expression. Plant Cell. 1990 Apr;2(4):291–299. doi: 10.1105/tpc.2.4.291. [DOI] [PMC free article] [PubMed] [Google Scholar]

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