A chimera of Urtica dioica agglutinin and tobacco chitinase displays both agglutination and chitinase activity

Plant Science

Volumn 148, Issue 2, 1999, Pages 121-129

  Does, Mirjam P ^a   Cornelissen, Ben J C ^a  

^a Institute for Molecular Cell Biology   (Netherlands)

Author keywords

Agglutination activity; Chitinase activity; Fusion protein; Stinging nettle lectin; Tobacco chitinase I

Indexed keywords

CHITINASE; HYBRID PROTEIN; PLANT LECTIN; SIGNAL PEPTIDE; TOBACCO; TRYPSIN;

ANIMAL CELL; ANTIGEN ANTIBODY REACTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CAULIFLOWER MOSAIC VIRUS; CONTROLLED STUDY; ENZYME ACTIVITY; ERYTHROCYTE; GENE SEQUENCE; NONHUMAN; PHYTOCHEMISTRY; PLANT LEAF; PLANT VIRUS; PROTEIN LOCALIZATION; RABBIT; STOP CODON; TRANSGENIC PLANT;

URTICA DIOICA;

EID: 0033615559     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(99)00128-4     Document Type: Article

References (35)

1. Peumans W.J., De Ley M., Broekaert W.F. An unusual lectin from stinging nettle (Urtica dioica) rhizomes. FEBS Lett. 177:1984;99-103.
2. Beintema J.J., Peumans W.J. The primary structure of stinging nettle (Urtica dioica) agglutinin: a two-domain member of the hevein family. FEBS Lett. 299:1992;131-134.
3. Does M.P., Ng D.K., Dekker H.L., Peumans W.J., Houterman P.M., Van Damme E.J.M., Cornelissen B.J.C. Characterization of Urtica dioica agglutinin isolectins and the encoding gene family. Plant Mol. Biol. 39:1999;335-347.
4. Archer B.L. The proteins of Hevea brasiliensis latex: isolation and characterization of crystalline hevein. Biochem. J. 75:1960;236-240.
5. K. Walujono, R.A. Scholma, J.J. Beintema, A. Mariono, A.M. Hahn, Amino acid sequence of hevein, Proceedings of the International Rubber Conference, Kuala Lumpur, Vol. 2, Rubber Research Institute, Malaysia, 1975, pp. 518-531.
6. Hom K., Gochin M., Peumans W.J., Shine N. Ligand-induced perturbations in Urtica dioica agglutinin. FEBS Lett. 361:1995;157-161.
7. Van Damme E.J.M., Peumans W.J. Isolectin composition of individual clones of Urtica dioica: evidence for phenotypic differences. Physiol. Plant. 71:1987;328-334.
8. Lerner D.R., Raikhel N.V. The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase. J. Biol.Chem. 267:1992;11085-11091.
9. Does M.P., Houterman P.M., Dekker H.L., Cornelissen B.J.C. Processing, targeting and antifungal activity of Urtica dioica agglutinin in transgenic tobacco. Plant Physiol. 120:1999;421-431.
10. Meins F. Jr, Fritig B., Linthorst H.J.M., Mikkelsen J.D., Neuhaus J.-M., Ryals J. Plant chitinase genes. Plant Mol. Biol. Reptr. 12:1994;S22-S28.
11. Neuhaus J.-M., Fritig B., Linthorst H.J.M., Meins F. Jr, Mikkelsen J.D., Ryals J. A revised nomenclature for chitinase genes. Plant Mol. Biol. Reptr. 14:1996;102-104.
12. Broekaert W.F., Van Parijs J., Leyns F., Joos H., Peumans W.J. A chitin-binding lectin from stinging nettle rhizomes with antifungal properties. Science. 245:1989;1100-1102.
13. Linthorst H.J.M., van Loon L.C., van Rossum C.M.A., Mayer A., Bol J.F., van Roekel J.S.C., Meulenhoff E.J.S., Cornelissen B.J.C. Analysis of acidic and basic chitinases from tobacco and petunia and their constitutive expression in transgenic tobacco. Mol. Plant Microbe Interact. 3:1990;252-258.
14. Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Jr Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol. Biol. 14:1990;357-368.
15. Neuhaus J.-M., Sticher L., Meins F. Jr, Boller T. A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc. Natl. Acad. Sci. U.S.A. 88:1991;10362-10366.
16. Melchers L.S., Sela-Buurlage M.B., Vloemans S.A., Woloshuk C.P., van Roekel J.S.C., Pen J., van den Elzen P.J.M., Cornelissen B.J.C. Extracellular targeting of the vacuolar tobacco proteins AP24, chitinase and β-1,3-glucanase in transgenic plants. Plant Mol. Biol. 21:1993;583-593.
17. Sticher L., Hofsteenge J., Neuhaus J.-M., Boller T., Meins F. Jr Posttranslational processing of a new class of hydroxyproline-containing proteins. Plant Physiol. 101:1993;1239-1247.
18. van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin. Mol. Gen. Genet. 232:1992;460-469.
19. Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins. Science. 257:1992;655-657.
20. Sela-Buurlage M.B., Ponstein A.S., Bres-Vloemans S.A., Melchers L.S., van den Elzen P.J.M., Cornelissen B.J.C. Only specific tobacco (Nicotiana tabacum) chitinases and β-1,3-glucanases exhibit antifungal activity. Plant Physiol. 101:1993;857-863.
21. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-termination inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74:1977;5463-5467.
22. Jongedijk E., Tigelaar H., van Roekel J.S.C., Bres-Vloemans S.A., Dekker I., van den Elzen P.J.M., Cornelissen B.J.C., Melchers L.S. Synergistic activity of chitinases and β-1,3-glucanases enhances fungal resistance in transgenic tomato plants. Euphytica. 85:1995;173-180.
23. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. Second ed. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
24. de Wit P.J.G.M., Spikman G. Evidence for the occurrence of race and cultivar-specific elicitors of necrosis in intercellular fluids of compatible interactions of Cladosporium fulvum and tomato. Physiol. Plant. Pathol. 21:1982;1-11.
25. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
26. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
27. Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
28. Wirth S.J., Wolf G.A. Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity. J. Microbiol. Methods. 12:1990;197-205.
29. Melchers L.S., Apotheker-de Groot M., van der Knaap J.A., Ponstein A.S., Sela-Buurlage M.B., Bol J.F., Cornelissen B.J.C., van den Elzen P.J.M., Linthorst H.J.M. A new class of tobacco chitinases homologous to bacterial exo-chitinases displays antifungal activity. Plant J. 5:1994;469-480.
30. Yun D.-J., Paino D'Urzo M., Abad L., Takeda S., Salzman R., Chen Z., Lee H., Hasegawa P.M., Bressan R.A. Novel osmotically induced antifungal chitinases and bacterial expression of an active recombinant isoform. Plant Physiol. 111:1996;1219-1225.
31. Brunner F., Stintzi A., Fritig B., Legrand M. Substrate specificities of tobacco chitinases. Plant J. 14:1998;225-234.
32. Iseli B., Boller T., Neuhaus J.-M. The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol. 103:1993;221-226.
33. M.B. Sela-Buurlage, In vitro sensitivity and tolerance of Fusarium solani towards chitinases and β-1,3-glucanases, Ph.D. thesis, Landbouwuniversiteit Wageningen, Wageningen, The Netherlands, 1996.
34. Van Parijs J., Broekaert W.F., Goldstein I.J., Peumans W.J. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta. 183:1991;258-264.
35. Broekaert W.F., Mariën W., Terras F.R.G., De Bolle M.F.C, Proost P., Van Damme J., Dillen L., Claeys M., Rees S.B., Vanderleyden J., Cammue B.P.A. Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry. 31:1992;4308-4314.