Site-directed mutagenesis of active site residues in a class I endochitinase from chestnut seeds

Glycobiology

Volumn 8, Issue 10, 1998, Pages 1021-1028

  Garcia Casado, Gloria ^a   Collada, Carmen ^a   Allona, Isabel ^a,b   Casado, Rosa ^a   Pacios, Luis F ^a   Aragoncillo, Cipriano ^a   Gomez, Luis ^a  

^a UNIVERSIDAD POLITÉCNICA DE MADRID   (Spain)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Antifungal protein; Chestnut; Chitin binding domain; Chitinase; Glycosyl hydrolase

Indexed keywords

AESCULUS HIPPOCASTANUM EXTRACT; ANTIFUNGAL AGENT; CHITIN; CHITINASE; ENDOCHITINASE; PLANT LECTIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANTIFUNGAL ACTIVITY; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PLANT SEED; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; TRICHODERMA VIRIDE;

AMINO ACID SEQUENCE; ANTIFUNGAL AGENTS; BASE SEQUENCE; BINDING SITES; CHITIN; CHITINASE; DNA PRIMERS; HYDROLYSIS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEEDS; SEQUENCE HOMOLOGY, AMINO ACID; TREES;

AESCULUS HIPPOCASTANUM; ESCHERICHIA COLI; FUNGI; HIPPOCASTANUM; TRICHODERMA VIRIDE; URTICA DIOICA;

EID: 0031691473     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/8.10.1021     Document Type: Article

References (44)

1. Allona, I., Collada, C., Casado, R., Paz-Ares, J. and Aragoncillo, C. (1996) Bacterial expression of an active class Ib chitinase from Castanea sativa cotyledons. Plant Mol. Biol., 32, 1171-1176.
2. Andersen, M.D., Jensen, A., Robertus, J.D., Leah, R. and Skriver, K. (1997) Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L.). Biochem. J., 322, 815-822.
3. Boller, T., Gehri, A., Mauch, F. and Vögeli, U. (1983) Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta, 157, 22-31.
4. Broekaert, W.H. Van Parijs, J., Leyns, F., Joos, H. and Peumans, W.J. (1989) A chitin-binding lectin from stinging nettle rhizomes with antifungal properties. Science, 245, 1100-1102.
5. Broekaert, W.F., Mariën, W., Terras, F.R.G., De Bolle, M.F.C., Proost, R. Van Damme, J., Dillen, L., Claeys, M., Rees, S.B., Van der Leyden, J. and Cammue, B.P.A. (1992) Antimicrobial peptides from Amuranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry, 31, 4308-4314.
6. Brogue, K., Chet, I., Holliday, M., Cressman, R., Biddle, P. Knowlton, S., Mauvais, C.J. and Broglie, R. (1991) Transgenic plants with enhanced resistance to the fungal pathogen Rhizoctonia solani. Science. 254, 1194-1197.
7. Brooks, B.R., Bruccoleri, R.E., Olafson, B.D., States, D.J., Swaminathar, S. and Karplus, M. (1983) CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem., 4, 187-217.
8. Chrispeels, M.J. and Raikhel, N.V. (1991) Lectins, lectin genes, and their role in plant defense. Plant Cell, 3, 1-9.
9. Collada, C., Casado, R., Fraile, A. and Aragoncillo, C. (1992) Basic endochitmases are major proteins in Castanea sativa cotyledons. Plant Physiol., 100, 778-783.
10. Collinge, D.B., Kragh, K.M., Mikkelsen, J.D., Nielsen, K.K., Rasmussen, U. and Vad, K. (1993) Plant chitinases. Plant J., 3, 31-40.
11. Fernandez-Pacios, L. (1997) Rendering of ray-traced images of molecular models on personal computers. Computers Chem., 21, 25-34.
12. Ford, L.O., Johnson, L.N., Mackin, P.A., Phillips, D.C. and Tjian, R. (1974) Crystal structure of a lysozyme-tetrasaccharide lactone complex. J. Mol. Biol., 88, 149-371.
13. Fukamizo, T., Koga, D. and Goto, S. (1995) Comparative biochemistry of chitinase-anomeric form of reaction products. Biosci. Biotechnol. Biochem., 59, 311-313.
14. Garcia-Casado, G., Sanchez-Monge, R., Chrispeels, M.J., Armentia, A., Salcedo, G. and Gomez, L. (1996) Role of complex asparagine-linked glycans in the allergenicity of plant glycoproteins. Glycobiology, 6,471-477.
15. Grison, R., Grezes-Besset, B., Schneider, M., Lucante, N., Olsen, L., Leguay, J.-J. and Toppan, A. (1996) Field tolerance to fungal pathogens of Brassica napus constitutively expressing chimeric chitinase gene. Nature Biotechnol., 14, 643-646.
16. Hart, P.J., Monzingo, A.F., Ready, M.P., Ernst, S.R. and Robertus, J.D. (1993) Crystal structure of an endochitinase from Hordeum vulgare L. seeds. J. Mol. Biol., 229, 189-193.
17. Hart, P.J., Pfluger, H.D., Monzingo, A.F., Hollis, T. and Robertus, J.D. (1995) The refined crystal structure of an endochitinase from Hordeum vulgare seeds at 1.8 Å resolution. J. Mol. Biol., 248, 402-413.
18. Henrissat, B. and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788.
19. Henrissat, B., Callebaut, I., Fabrega, S., Lehn, P., Mornon, J.-P. and Davies, G. (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA, 92, 7090-7094.
20. Higgins, D.C. and Sharp, P.M. (1988) CLUSTAL: a package for performing multiple sequence alignments on a microcomputer. Gene, 73, 237-244.
21. Holm, L. and Sander, C. (1994) Structural similarity of plant chitinase and lysozymes from animal and phage. An evolutionary connection. FEBS Lett., 340, 129-132.
22. Iseli, B., Boller, T. and Neuhaus, J.-M. (1993) The N-terminal cysteine-richdomain of tobacco class I citinase is esential for chitin binding but not for catalytic or antifungal activity. Plant Physiol., 103, 221-226.
23. Iseli, B., Armand, S., Boller, T. Neuhaus, J.-M. and Henrissat, B. (1996) Plant chitinases use two different hydrolytic mechanisms. FEBS Lett., 382, 186-188.
24. Jach, G., Görnhardt, B., Mundy, J., Logemann, J., Pinsdorf, E., Leah, R., Schell, J. and Maas, C. (1995) Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J., 8, 97-109.
25. Kraulis, J.P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
26. Kuroki, R., Weaver, L.H. and Matthews, B.W. (1995) Structure-based design of a lysozyme with altered catalytic activity. Nature Struct. Biol., 2, 1007-1011.
27. Landt, O., Grunert, H.P. and Hahn, U. (1990) A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene, 96, 125-128.
28. Malcolm, B.A., Rosenberg, S., Corey, M.J., Allen, J.S., de Baetselier, A. and Kirsch, J.F. (1989) Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proc. Natl. Acad. Sci. USA. 86, 133-137.
29. Matsumura, I. and Kirsch, J.F. (1996) Is aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis. Biochemistry, 35, 1890-1896.
30. Mauch, F., Mauch-Mani, b. and Boller, T. (1988) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combination of chitinase and ß-1,3-glucanase. Plant Physiol., 88, 936-942.
31. Meins, E. Fritig, B., Linthorst, H.J.M., Mikkelsen, J.D., Neuhaus, J.-M. and Ryals, J. (1994) Plant chitinase genes. Plant Mol. Biol. Rep., 12, 522-528.
32. Monzingo, A.F., Marcotte, E.M., Hart, P.J., Robertus, J.D. (1996) Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core. Nature Struct. Biol., 3, 123-140.
33. Peitsch, M. (1995) Protein modeling by e-mail. Bio/Technology, 13, 658-660.
34. Perrakis, A., Tews, I., Dauter, Z., Oppenheim, A.M., Chet, I., Wilson, K.S. and Vorgias, C.E. (1994) Crystal structure of a bacterial chitinase at 2.3 Å resolution. Structure, 2, 1169-1180.
35. Raikhel, N.V., Lee, H.-I. and Broekaert, W.F. (1993) Structure and function of chitin-binding proteins. Annu. Rev. Plant Physiol. Plant Mol. Biol., 44, 591-615.
36. Schlumbaum, A., Mauch, F. Vögeli, U. and Boller, T. (1986) Plant chitinases are potent inhibitors of fungal growth. Nature, 324, 365-367.
37. Shinshi, H., Neuhaus, J.-M., Ryals, J. and Meins, F. (1990) 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, 357-368.
38. Song, H.K. and Suh, S.W. (1996) Refined structure of the chitinase from barley seeds at 2.0 Å resolution. Acta Crystallogr., D52, 289-298.
39. Terwisscha van Scheltinga, M. Hennig, M. and Dijkstra, B.W. (1996) The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and stracutre motifs of glycosyl hydrolase family 18. J. Mol. Biol., 262, 243-257.
40. Van Parijs, J., Broekaert, W.F., Goldstein, I.J. and Peumans, W.J. (1991) Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta, 183, 258-264
41. Verburg, J.G., Smith, C.E., Lisek, C.A. and Huynh, Q.K. (1992) Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated rom Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide. J. Biol. Chem., 267, 3886-3893.
42. Verburg, J.G., Rangwala, S.H., Samac, D.A., Luckow, V.A. and Huynh, Q.K. (1993) Examination of the role of tyrosine-174 in the catalytic mechanism of the Arabidopsis thaliana chitinase: comparison of variant chitinases generated by site-directed mutagenesis and expression in insect cells using baculovirus vectors. Arch. Biochem. Biophys., 300, 223-230.
43. Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M. and Tanaka, H. (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem., 268, 18567-18572.
44. Wirth, S.J. and Wolf, G.A. (1990) Dye-labeled substrates for the assay and detection of chitinase and lysozyme activity. J. Microbiol. Methods, 12, 197-205.