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. 1986 Oct;83(19):7277–7281. doi: 10.1073/pnas.83.19.7277

Molecular characterization and phylogenetic studies of a wound-inducible proteinase inhibitor I gene in Lycopersicon species.

J S Lee, W E Brown, J S Graham, G Pearce, E A Fox, T W Dreher, K G Ahern, G D Pearson, C A Ryan
PMCID: PMC386699  PMID: 3463966

Abstract

A gene coding for proteinase inhibitor I, whose expression is induced in tomato leaves (Lycopersicon esculentum L. var. Bonny Best) in response to wounding or insect attacks, was isolated from a genomic library and characterized. The nucleotide sequence revealed that the gene is complete and encodes the sequence of an inhibitor I cDNA that was previously isolated from a cDNA library prepared from wound-induced mRNA from tomato leaves. This gene is located 13.1 kilobase pairs (kbp) upstream from an inhibitor II gene. The wound-inducible gene is interrupted by two intervening sequences of 445 and 404 bp, situated within the codons of amino acids 17 and 47, respectively, of the open reading frame. In addition to the presence of putative regulatory sequences, TATAAA and CCACT, two copies of an imperfect direct repeat approximately 100 bp long were identified in the 5'-flanking region. Phylogenetic comparisons of wound-inducible inhibitor I genes within the genomes of various Lycopersicon species revealed that the repeat is found in seven ancestral species of tomato.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benton W. D., Davis R. W. Screening lambdagt recombinant clones by hybridization to single plaques in situ. Science. 1977 Apr 8;196(4286):180–182. doi: 10.1126/science.322279. [DOI] [PubMed] [Google Scholar]
  2. Bishop P. D., Pearce G., Bryant J. E., Ryan C. A. Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves. Identity and activity of poly- and oligogalacturonide fragments. J Biol Chem. 1984 Nov 10;259(21):13172–13177. [PubMed] [Google Scholar]
  3. Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
  4. Bryant J., Green T. R., Gurusaddaiah T., Ryan C. A. Proteinase inhibitor II from potatoes: isolation and characterization of its protomer components. Biochemistry. 1976 Aug 10;15(16):3418–3424. doi: 10.1021/bi00661a004. [DOI] [PubMed] [Google Scholar]
  5. Coruzzi G., Broglie R., Edwards C., Chua N. H. Tissue-specific and light-regulated expression of a pea nuclear gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase. EMBO J. 1984 Aug;3(8):1671–1679. doi: 10.1002/j.1460-2075.1984.tb02031.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dean C., Elzen P., Tamaki S., Dunsmuir P., Bedbrook J. Differential expression of the eight genes of the petunia ribulose bisphosphate carboxylase small subunit multi-gene family. EMBO J. 1985 Dec 1;4(12):3055–3061. doi: 10.1002/j.1460-2075.1985.tb04045.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fyrberg E. A., Mahaffey J. W., Bond B. J., Davidson N. Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Cell. 1983 May;33(1):115–123. doi: 10.1016/0092-8674(83)90340-9. [DOI] [PubMed] [Google Scholar]
  8. Gillies S. D., Morrison S. L., Oi V. T., Tonegawa S. A tissue-specific transcription enhancer element is located in the major intron of a rearranged immunoglobulin heavy chain gene. Cell. 1983 Jul;33(3):717–728. doi: 10.1016/0092-8674(83)90014-4. [DOI] [PubMed] [Google Scholar]
  9. Graham J. S., Pearce G., Merryweather J., Titani K., Ericsson L., Ryan C. A. Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing. J Biol Chem. 1985 Jun 10;260(11):6555–6560. [PubMed] [Google Scholar]
  10. Green T. R., Ryan C. A. Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism against Insects. Science. 1972 Feb 18;175(4023):776–777. doi: 10.1126/science.175.4023.776. [DOI] [PubMed] [Google Scholar]
  11. Gustafson G., Ryan C. A. Specificity of protein turnover in tomato leaves. Accumulation of proteinase inhibitors, induced with the wound hormone, PIIF. J Biol Chem. 1976 Nov 25;251(22):7004–7010. [PubMed] [Google Scholar]
  12. Henikoff S. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 1984 Jun;28(3):351–359. doi: 10.1016/0378-1119(84)90153-7. [DOI] [PubMed] [Google Scholar]
  13. Hightower R. C., Meagher R. B. Divergence and differential expression of soybean actin genes. EMBO J. 1985 Jan;4(1):1–8. doi: 10.1002/j.1460-2075.1985.tb02309.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kuo T. M., Pearce G., Ryan C. A. Isolation and characterization of proteinase inhibitor I from etiolated tobacco leaves. Arch Biochem Biophys. 1984 May 1;230(2):504–510. doi: 10.1016/0003-9861(84)90430-2. [DOI] [PubMed] [Google Scholar]
  15. Laskowski M., Jr, Kato I. Protein inhibitors of proteinases. Annu Rev Biochem. 1980;49:593–626. doi: 10.1146/annurev.bi.49.070180.003113. [DOI] [PubMed] [Google Scholar]
  16. Leder P., Tiemeier D., Enquist L. EK2 derivatives of bacteriophage lambda useful in the cloning of DNA from higher organisms: the lambdagtWES system. Science. 1977 Apr 8;196(4286):175–177. doi: 10.1126/science.322278. [DOI] [PubMed] [Google Scholar]
  17. Melville J. C., Ryan C. A. Chymotrypsin inhibitor I from potatoes. Large scale preparation and characterization of its subunit components. J Biol Chem. 1972 Jun 10;247(11):3445–3453. [PubMed] [Google Scholar]
  18. Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Nelson C. E., Ryan C. A. In vitro synthesis of pre-proteins of vacuolar compartmented proteinase inhibitors that accumulate in leaves of wounded tomato plants. Proc Natl Acad Sci U S A. 1980 Apr;77(4):1975–1979. doi: 10.1073/pnas.77.4.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
  21. Plunkett G., Senear D. F., Zuroske G., Ryan C. A. Proteinase inhibitors I and II from leaves of wounded tomato plants: purification and properties. Arch Biochem Biophys. 1982 Feb;213(2):463–472. doi: 10.1016/0003-9861(82)90572-0. [DOI] [PubMed] [Google Scholar]
  22. Ryan C. A. Assay and Biochemical Properties of the Proteinase Inhibitor-inducing Factor, a Wound Hormone. Plant Physiol. 1974 Sep;54(3):328–332. doi: 10.1104/pp.54.3.328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ryan C. A. Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies. Anal Biochem. 1967 Jun;19(3):434–440. doi: 10.1016/0003-2697(67)90233-3. [DOI] [PubMed] [Google Scholar]
  24. Seemüller U., Eulitz M., Fritz H., Strobl A. Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis. Hoppe Seylers Z Physiol Chem. 1980 Dec;361(12):1841–1846. [PubMed] [Google Scholar]
  25. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  26. Swank R. T., Munkres K. D. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Anal Biochem. 1971 Feb;39(2):462–477. doi: 10.1016/0003-2697(71)90436-2. [DOI] [PubMed] [Google Scholar]
  27. Trautman R., Cowan K. M., Wagner G. G. Data processing for radial immunodiffusion. Immunochemistry. 1971 Oct;8(10):901–916. doi: 10.1016/0019-2791(71)90429-0. [DOI] [PubMed] [Google Scholar]
  28. Wahl G. M., Stern M., Stark G. R. Efficient transfer of large DNA fragments from agarose gels to diazobenzyloxymethyl-paper and rapid hybridization by using dextran sulfate. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3683–3687. doi: 10.1073/pnas.76.8.3683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Walker-Simmons M., Ryan C. A. Immunological Identification of Proteinase Inhibitors I and II in Isolated Tomato Leaf Vacuoles. Plant Physiol. 1977 Jul;60(1):61–63. doi: 10.1104/pp.60.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Weiher H., König M., Gruss P. Multiple point mutations affecting the simian virus 40 enhancer. Science. 1983 Feb 11;219(4585):626–631. doi: 10.1126/science.6297005. [DOI] [PubMed] [Google Scholar]
  31. Wickens M., Stephenson P. Role of the conserved AAUAAA sequence: four AAUAAA point mutants prevent messenger RNA 3' end formation. Science. 1984 Nov 30;226(4678):1045–1051. doi: 10.1126/science.6208611. [DOI] [PubMed] [Google Scholar]

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