Systemin

Chemistry: molecular biology and microbiology – Vector – per se

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

536 236, 514 12, 514 13, C12N 1582, C12N 1529

Patent

active

060227397

ABSTRACT:
Systemin, an 18 amino acid peptide hormone and first polypeptide hormone found in plants, induces expression of defense genes in plants wounded mechanically or by predators including herbivores, insects, bacteria and viruses. The precursor for systemin is encoded as a 200 amino acid prosystemin molecule that has the systemin peptide sequence located near the carboxyl-terminus. Both a 951 bp cDNA for prosystemin and 4526 bp genomic DNA were cloned and the organization of the gene was determined. Transgenic plants constructed with antisense prosystemin DNA fail to mount a defensive response to wounding. Transgenic plants constructed with increased copy number of prosystemin genes exhibit increased resistance to wounding. Insect larval that feed on transgenic plants constructed with increased copy number of prosystemin genes exhibit decreased growth weight compared to larval that feed on wild type plants.

REFERENCES:
patent: 4394443 (1983-07-01), Weissman et al.
patent: 5378819 (1995-01-01), Ryan et al.
Baydoun, E.A. et al., "The immobility Of Pectic Substances In Injured Tomato Leaves And Its Bearing On The Identity Of The Wound Hormone," Planta 165:269-276 (1985).
Becraft, P.W. et al., "CRINKLY4: A TNFR-Like Receptor Kinase Involved in Maize Epidermal Differentiation," Science 273:1046-1409 (1996).
Bergey, D.R. et al., "Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animals," Proc Natl Acad Sci USA 93:12053-12058 (1996).
Beuning, L.L. et al., "Evolution of the Proteinase Inhibit I Family and Apparent Lack of Hypervariability in the Proteinase Contact Loop," J Mol Evol 39:644-654 (1994).
Bidlingmeyer, B.A. et al., "Rapid Analysis Of Amino Acids Using Pre-Column Derivatization," Journal Of Chromatography 336:93-104 (1984).
Bowles, D.J., "Defense-Related Proteins In Higher Plants," Annu. Rev. Biochem. 59-873-907 (1990).
Bradshaw, H.D. et al., "Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors," Plant Molecular Biology 14:51-59 (1989).
Brown, W.E. et al., "Isolation and Characterization of a Wound-Induced Trypsin Inhibitor from Alfalfa Leaves," Biochemistry 23(15):3418-3422 (1984).
Brown, W.E. et al., "Wound-Induced Typsin Inhibitor in Alfalfa Leaves: Identity as a Member of the Bowman-Birk Inhibitor Family," Biochemistry 24(9):2105-2108 (1985).
Chasan, R., "Plant Molecular Biology Blossoms in the Desert," The Plant Cell 3:1255-1262 (1991).
Chessin, M. et al., "Alarm Systems In Higher Plants," The Botanical Review 56:193-235 (1990).
Cleveland, T.E. et al., "Molecular Characterization of a wound-inducible inhibitor I gene from potato and the processing of its mRNA and protein," Plant Mol Biol 8:199-207 (1985).
Constabel, C.P. et al., "Systemin activates synthesis of wound-inducible tomato leaf polyphenol oxidase via the octadecanoid defense signaling pathway," PNAS (USA) 92:407-411 (1995).
Culver, J.N. et al., "Tobacco Mosaic Virus Elicitor Coat Protein Genes Produce A Hypersensitive Phenotype In Transgenic Nicotiana sylvestris Plants," Molecular Plant-Microbe Interactions 4(5):458-463 (1991).
Davies, E., "Action potentials a multifunctional signals in plants: a unifying hypothesis to explain apparently disparate wound responses," Plant, Cell and Environment 10:623-631 (1987).
Douglass, J. et al., "Polyprotein Gene Expression: Generation of Diversity of Neuroendocrine Peptides," Ann. Rev. Biochem. 53:665-715 (1984).
Dreyer, D.L. et al., "Chemical basis of host-plant resistance to aphids," Plant, Cell and Environment 10:353-361 (1987).
Farmer, E.E. et al., "Interplant communication: Airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves," Proc. Natl. Acad. Sci. (USA) 87:7713-7716 (1990).
Frohman, M., "Race: Rapid Amplification Of cDNA Ends," In Innis MA (ed), PCR Protocols: A Guide to Methods and Applications, pp. 28-37. Academic Press, San Diego, CA (1990).
Graham, J.S. et al., "Wound-induced Proteinase Inhibitors from Tomato Leaves," J. Biol. Chem. 260(11):6561-6564 (1985).
Graham, J.S. et al., "Regulation of synthesis of proteinase inhibitors I and II mRNAs in leaves of wounded tomato plants," Planta 169:399-405 (1986).
Graham, J.S. et al., "Wound-induced Proteinase Inhibitors from Tomato Leaves," The Journal Of Biological Chemistry 260(11):6555-6560 (1985).
Green, T.R. et al., "Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism Against Insects," Science 175:776-777 (1972).
Hammond-Kosack, K.E. et al., "Systemic accumulation of novel proteins in the apoplast of the leaves of potato plants following root invasion by the cyst-nematode Globodera rostochiensis," Physiological and Molecular Plant Pathology 35:495-506 (1989).
Harris, R.B., "Processing of Pro-hormone Precursor Proteins," Archives Of Biochemistry And Biophysics 275(2):315-333 (1989).
Hilder, V.A. et al., "A novel mechanism of insect resistance engineered into tobacco," Nature 330:160-163 (1987).
Hopp, T.P. et al., "Prediction of protein antigenic determinants from amino acid sequences," Proc. Natl. Acad. Sci (USA) 78(6):3824-3828 (1981).
Hummel, B., "A Modified Spectrophotonetric Determination Of Chymotrypsin, Trypsin, And Thrombin," Can J Biochem Physiol 37:1393-1399 (1959).
Johnson, R. et al., "Expression of proteinase inhibitors I and II in transgenic tobacco plants: Effects on natural defense against Manduca sexta larvae," Proc. Natl. Acad. Sci. USA 86:9871-9875 (1989).
Jung, L.J. et al., "Peptide Processing and Targeting in the Neuronal Secretory Pathway," Science 251:1330-1335 (1991).
King, R.W. et al., "Enhancement of Phloem Exudation from Cut Petioles by Chelating Agents," Plant Physiol 53:96-103 (1974).
Kopp, M. et al., "Host Pathogen Interactions," Plant Physiol. 90:208-216 (1989).
Kuc, J. et al., "Fungal Regulation Of Disease Resistance Mechanisms In Plants," Mycologia 76(5):767-784 (1984).
Lutcke, H.A. et al., "Selection of AUG initiation condons differs in plants and animals," The EMBO Journal 6(1):43-48 (1987).
Maniatis, T. et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring, NY pp. 387-389 (1982).
Marchuk, D. et al., "Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products," Nuc Acids Res 19:1154 (1991).
McGurl B. et al., "The organization of the prosystemin gene," Plant Mol Biol 20:405-409 (1992).
McGurl, B. et al., "Overexpression of the prosystemin gene in transgenic tomatoe plants generates a systemic signal that constitutively induces proteinase inhibitor synthesis," PNAS (USA) 91:9799-9802 (1994).
McGurl, B. et al., "Structure, Expression, and Antisense Inhibition of the Systemin Precursor Gene," Science 255:1570-1573 (1992).
Pearce, G. et al., "A Polypeptide from Tomato Leaves Induces Wound-Inducible Proteinase Inhibitor Proteins," Science 253:895-898 (1991).
Pearce, G. et al., "Purification and Characterization from Tobacco (Nicotiana tabacum) Leaves of Six Small, Wound-Inducible, Proteinase Isoinhibitors of the Potato Inhibitor II Family," Plant Physiol 102:639-644 (1993).
Pearce, G. et al., "Structure-Activity of Deleted and Substituted Systemin, an 18-Amino Acid Polypeptide Inducer of Plant Defensive Genes," J Biol Chem 268:212-216 (1993).
Pen-Cortes, H. et al., "Systemic induction of proteinase-inhibitor-II gene expression in potato plants by wounding," Planta 174:84-89 (1988).
Pen-Cortes, H. et al., "Abscisic acid is involved in the wound-induced expression of the proteinase inhibitor II gene in potato and tomato," Proc. Natl. Acad. Sci (USA) 86:9851-9855 (1989).
Realini, C. et al., "Proposed roles in protein-protein association and presentation of peptides by MHC Class I receptors," FEBS Let 348:109-113 (1994).
Roby, D. et al., "Cell surfaces in plant micro-organism interactoins, VIII. Increased proteinase inhibitor activity in melon plants in response to infection by Colletotrichum lagenarium or to treatment with an elicitor fraction from this fungus," Physiological and Molecular Plant Pathology 30:453-460 (1987).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Systemin does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Systemin, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Systemin will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-1680263

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.