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Cloning and characterization of a cathepsin D inhibitor gene from Solanum tuberosum L.

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Abstract

A DNA clone encoding a cathepsin D inhibitor CathInh was isolated from a potato genomic library using a CathInh cDNA as hybridization probe. The amino acid sequence of the coding region is nearly identical with a CathInh cDNA and CathInh proteins previously isolated from a tuber-specific cDNA library and from tubers, respectively. Analysis of GUS activity resulting from expression of chimeric CathInh promoter-GUS genes in transgenic potato plants revealed expression exclusively confined to potato tubers. No GUS activity could be detected in any other organ of the transgenic plants either constitutively or after wounding or treatment with abscisic and jasmonic acid (JA). Interestingly, part of the promoter region of the CathInh gene, essential for GUS activity in tubers, shows striking similarity to promoter regions of tuber-specific class I patatin genes.

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References

  1. Ryan C: Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Annu Rev Phytopath 28: 425–449 (1990).

    Google Scholar 

  2. Santarius K, Belitz HD: Proteinase activity in potato plants. Planta 141: 145–153 (1978).

    Google Scholar 

  3. Hildmann T, Ebneth M, Pena-Cortés H, Sánchez-Serrano JJ, Willmitzer L: General roles of abscisic and jasmonic acids in gene.activation as a result of mechanical wounding. Plant Cell 4: 1157–1170 (1992).

    Google Scholar 

  4. Abe K, Emore Y, Kondo H, Suzuki K, Arai S: Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds. J Biol Chem 262: 16793–16797 (1987).

    Google Scholar 

  5. Strukelj B, Pungercar J, Ritonja A, Krizaj, Gubensek F, Kregar I, Turk V: Nucleotide and deduced amino acid sequence of an aspartic proteinase inhibitor homologue from potato tubers (Solanum tuberosum L.). Nucl Acids Res 18: 4605 (1990).

    Google Scholar 

  6. Graham J, Pearce G, Merryweather J, Titani K, Ericsson L, Ryan CA: Wound-induced proteinase inhibitors from tomato leaves. The cDNA-deduced primary structure of pre-inhibitor II. J Biol Chem 260: 6561–6564 (1985).

    Google Scholar 

  7. Sánchez-Serrano J, Schmidt R, Schell J, Willmitzer L: Nucleotide sequence of proteinase inhibitor II encoding cDNA of potato (Solanum tuberosum) and its mode of expression. Mol Gen Genet 203: 15–20 (1986).

    Google Scholar 

  8. Peña-Cortés H, Willmitzer L, Sánchez-Serrano JJ: Abscisic acid mediates wound induction but not developmental-specific expression of the proteinase inhibitor II gene family. Plant Cell 3: 963–972 (1991).

    Google Scholar 

  9. Farmer EE, Ryan C: Interplant communication: Airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves. Proc Natl Acad Sci USA 87: 7713–7716 (1990).

    Google Scholar 

  10. Murashige T, Skoog F: A revised medium for rapid growth and biassays with tobacco tissue cultures. Physiol Plant 15: 473–497 (1962).

    Google Scholar 

  11. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd edition, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1989).

    Google Scholar 

  12. Deblaere R, Bytebier B, De Greve H, Debroeck FM, Schell J, Van Montagu M, Leemans J: Efficient octopine Ti-plasmid derived vectors for Agrobacterium-mediated gene transfer. Nucl Acids Res 13: 4777–4788 (1985).

    Google Scholar 

  13. Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).

    Google Scholar 

  14. Keilová H, Homásek V: Isolation and some properties of cathepsin D inhibitor from potatoes. Coll Czech Chem Commun 41: 489–497 (1976).

    Google Scholar 

  15. Logemann J, Schell J, Willmitzer L: Improved method for the isolation of RNA from plant tissues. Anal Biochem 163: 21–26 (1987).

    Google Scholar 

  16. Jefferson RA: Assaying chimeric genes in plants: The GUS gene fusion system. Plant Mol Biol Rep 5: 387–407 (1987).

    Google Scholar 

  17. Höfgen R, Willmitzer L: Storage of competent cells for Agrobacterium transformation. Nucl Acids Res 16: 9877 (1988).

    Google Scholar 

  18. Rogers SO, Bendich AJ: Extraction of DNA from milligram amounts of fresh, herbarium and mummified plant tissues. Plant Mol Biol 5: 69–76 (1985).

    Google Scholar 

  19. Bradford MM: Rapid and quantitative method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–252 (1976).

    Google Scholar 

  20. Mares M, Meloun B, Pavlik M, Kostka V, Baudys M: Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family. FEBS Lett 251: 94–98 (1989).

    Google Scholar 

  21. Ritonja A, Krizaj I, Mesko P, Kopitar M, Lucvnik P, Strukelj B, Pungercar J, Buttle DJ, Barrett AJ, Turk V: The amino acid sequence of a novel inhibitor of cathepsin D from potato. FEBS Lett 267: 13–15 (1990).

    Google Scholar 

  22. Keil M, Sánchez-Serrano JJ, Willmitzer L: Both wound-inducible and tuber-specific expression are mediated by the promoter of a single member of the potato proteinase inhibitor II gene family. EMBO J 8: 1323–1330 (1989).

    Google Scholar 

  23. Keil M, Sánchez-Serrano JJ, Schell J, Willmitzer L: Localization of elements important for the wound-inducible expression of a chimeric potato proteinase inhibitor II-CAT gene in transgenic tobacco plants. Plant Cell 2: 61–70 (1990).

    Google Scholar 

  24. Lorberth R, Dammann C, Ebneth M, Amati S, Sánchez-Serrano JJ: Promoter elements involved in environmental and developmental control of potato proteinase inhibitor II expression. Plant J 2: 477–486 (1992).

    Google Scholar 

  25. Kim S-R, Choi J-L, Costa MA, An G: Identification of G-box sequence as an essential element for methyl jasmonate response of potato proteinase inhibitor II promoter. Plant Physiol 99: 627–631 (1992).

    Google Scholar 

  26. Rocha-Sosa M, Sonnewald U, Frommer W, Stratmann M, Schell J, Willmitzer L: Both developmental and metabolic signals activate the promoter of a class I patatin gene (1989).

  27. Lui XJ, Rocha-Sosa M, Hummel S, Willmitzer L, Frommer WB: A detailed study of the regulation and evolution of the classes of patatin genes in Solanum tuberosum L. Plant Mol Biol 17: 1139–1154 (1991).

    Google Scholar 

  28. Liu XJ, Prat S, Willmitzer L, Frommer WB: Cis regulatory elements directing tuberspecific and sucrose-inducible expression of a chimeric class I patatin promoter/ GUS-gene fusion. Mol Gen Genet 223: 401–406 (1990).

    Google Scholar 

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Herbers, K., Prat, S. & Willmitzer, L. Cloning and characterization of a cathepsin D inhibitor gene from Solanum tuberosum L.. Plant Mol Biol 26, 73–83 (1994). https://doi.org/10.1007/BF00039521

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  • DOI: https://doi.org/10.1007/BF00039521

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