Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 67, 2003 - Issue 4
Journal homepage
406
Views
25
CrossRef citations to date
0
Altmetric
Original Articles

Cloning, Expression, and Characterization of an Antifungal Chitinase from Leucaena leucocephala de Wit

Mana KAOMEKInstitute of Science, Suranaree University of TechnologyNakhon Ratchasima 30000, Thailand;Faculty of Science and Technology Rajabhat InstitutePecthburiwittayalongkorn Pathumthani, 13180, Thailand
,
Kouichi MIZUNOInstitute of Agricultural and Forest Engineering, University of TsukubaIbaraki 305-8572, Japan;Faculty of Bioresource Sciences, Akita Prefectural UniversityAkita City, Akita 010-0195, Japan
,
Tatsuhito FUJIMURAInstitute of Agricultural and Forest Engineering, University of TsukubaIbaraki 305-8572, Japan
,
Poonsook SRIYOTHAInstitute of Science, Suranaree University of TechnologyNakhon Ratchasima 30000, Thailand
&
James R. Ketudat CAIRNSInstitute of Science, Suranaree University of TechnologyNakhon Ratchasima 30000, Thailand;Biochemistry Laboratory, Chulabhorn Research Institute
Pages 667-676 | Received 19 Apr 2002, Accepted 14 Dec 2002, Published online: 22 May 2014

  • 1) Davis, B., and Eveleigh, D. E., Chitinases: occurrence, production and immobilization. In “Chitin, Chitosan and Related Enzymes”, ed. Zikakis, J. P., Academic Press, New York, pp. 160-179 (1984).
  • 2) Collinge, D. B., Kragh, K. M., Mikkelsen, I. D., Nieler, K. K., Rasmussen, U., and Vad, K., Plant chitinases. Plant J., 3, 31-40 (1993).
  • 3) Kramer, K. J., Corpuz, L., Choi, H. K., and Muthukrishnan, S., Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinase of Manduca sexta. Insect Biochem. Mol. Biol., 23, 691-701 (1993).
  • 4) Bowles, D., Defense-related proteins in higher plants. Annu. Rev. Biochem., 59, 873-907 (1990).
  • 5) Linthorst, H. J. M., Pathogenesis-related proteins of plants. Crit. Rev. Plant Sci., 10, 123-150 (1991).
  • 6) Verburg, J. G., and Huynh, Q. K., Purification and characterization of an antifungal chitinase from Arabidopsis thaliana. Plant Physiol., 95, 450-455 (1991).
  • 7) Hakala, B. E., White, C., and Recklies, A. D., Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J. Biol. Chem., 268, 25803-25810 (1993).
  • 8) Broglie, K., Chet, I., Hollyday, M., Cressman, R., Biddle, P., Knowlton, S., Mauvais, C. J., and Broglie, R., Transgenic plants with enhanced resistance to the fungal pathogen Rhizoctonia solani. Science, 254, 1194-1197 (1991).
  • 9) Nishizawa, Y., Nishio, Z., Nakazono, K., Soma, M., Nakajima, E., Ugaki, M., and Hibi, T., Enhanced resistance to blast (Magnaporthe grisea) in transgenic Japonica rice by constitutive expression of rice chitinase. Theor. Appl. Genet., 99, 383-390 (1999).
  • 10) Boller, T., Ethylene and the regulation of antifungal hydrolases in plants. In “Surveys of Plant Molecular and Cell Biology” vol. 5, ed. Miflin, B. J., Oxford University Press, Oxford, UK, pp. 145-174 (1988).
  • 11) Broglie, K. E., Gaynor, J. J., and Broglie, R. M., Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc. Natl. Acad. Sci. USA, 83, 6820-6824 (1986).
  • 12) Watanabe, A., Nong, V. H., Zhang, D., Arahira, M., Yeboah, N. A., Udaka, K., and Fukazawa, C., Molecular cloning and ethylene-inducible expression of Chib1 chitinase from Soybean (Glycine max (L.) Merr.). Biosci. Biotechnol. Biochem., 63, 251-256 (1999).
  • 13) Staehelin, C., Schultze, M., Kondorosi, E., Mellor, R. B., Boller, T., and Kondorosi, A., Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases. Plant J., 5, 319-330 (1994).
  • 14) Zhong, R., Kays, S. J., Schroeder, B. P., and Ye, Z.-H., Mutation of a chitinase-like gene causes ectopic deposition of lignin, aberrant cell shapes, and overproduction of ethylene. Plant Cell, 14, 165-179 (2002).
  • 15) De Jong, A. J., Heidstra, R., Spaink, H. P., Hartog, M. V., Meijer, E. A., Hendriks, T., Lo Schiavo, F., Terzi, M., Bisseling, T., Van Kammen, A., and De Vries, S. C., Rhizobium lipooligosaccharides rescue a carrot somatic embryo mutant. Plant Cell, 5, 615-620 (1993).
  • 16) Henrissat, B., Coutinho, P. M., and Davies, G. J., A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana. Plant Mol. Biol., 47, 55-72 (2001).
  • 17) Beintema, J. J., Structural features of plant chitinases and chitin-binding proteins. FEBS Lett., 350, 159-163 (1994).
  • 18) Meins, F., Fritig, B. J., Linthorst, H. J. M., Mikkelsen, J. D., Neuhaus, J.-M., and Ryals, J., Plant chitinase genes. Plant Mol. Biol. Rep., 12, S22-S28 (1994).
  • 19) Henrissat, B., and Bairoch, A., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
  • 20) Hawtin, R. E., Arnold, K., Ayres, M. D., Zanotto, P. M., Howard, S. C., Gooday, G. W., Chappell, L. H., Kitts, P. A., King, L. A., and Possee, R. D., Identification and preliminary characterization of a chitinase gene in the Autographa californica nuclear polyhedrosis virus genome. Virology, 212, 673-685 (1995).
  • 21) Watanabe, T., Kanai, R., Kawase, T., Tanabe, T., Mitsutomi, M., Sakuda, S., and Miyashita, K., Family 19 chitinases of Streptomyces species: characterization and distribution. Microbiology, 145, 3353-3363 (1999).
  • 22) Shimosaka, M., Fukumori, Y., Narita, T., Zhang, X., Kodaira, R., Nogawa, M., and Okazaki, M., The bacterium Burkholderia gladioli strain CHB101 produces two different kinds of chitinases belonging to families 18 and 19 of the glycosyl hydrolases. J. Biosci. Bioeng., 91, 103-105 (2001).
  • 23) Andersen, N. H., Cao, B., Rodriguez-Romero, A., and Arreguin, B., Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif. Biochemistry, 32, 1407-1422 (1993).
  • 24) Song, H. K., Hwang, K. Y., Kim, K. K., and Suh, S. W., Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds. Proteins, 17, 107-109 (1993).
  • 25) Shishi, H., Neuhans, J.-M., Ryals, I., and Meins, F., Structure of 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 (1990).
  • 26) Yamagami, T., Tanigama, M., Ishiguro, M., and Funatso, G., Complete amino acid sequence of chitinase-A from leaves of pokeweed (Phytolacca americana). Biosci. Biotechnol. Biochem., 62, 825-828 (1998).
  • 27) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
  • 28) Boller, T., and Mauch, F., Colorimetric assay for chitinase. Methods Enzymol., 161, 430-435 (1988).
  • 29) Andrew, A. T., “Electrophoresis: Theory, Techniques, and Biochemical and Clinical Application” 2nd Ed., Oxford University Press, New York (1986).
  • 30) Feng, D. F., and Doolittle, R. F., Progressive alignment of amino acid sequences and construction of phylogenetic trees from them. Methods Enzymol., 266, 226-368 (1996).
  • 31) Clendennen, S. K., and May, G. D., Differenttial gene expression in ripening banana fruit. Plant Physiol., 115, 463-469 (1997).
  • 32) Frohman, M. A., and Martin, G. R., Rapid amplification of cDNA ends using nested primers. Techniques, 1, 165-170 (1989).
  • 33) Gubler, U., and Hoffman, A., A simple and very efficient method for generating cDNA libraries. Gene, 25, 263-269 (1983).
  • 34) Altschul, S. F., Thomas, L. M., Alejandro, A. S., Jinghui, Z., Zheng, Z., Webb, M., and David, J. L., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res., 25, 3389-3402 (1997).
  • 35) Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G., Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engineering, 10, 1-6 (1997).
  • 36) Anderson, M. D., Jensen, A., Robertus, J. D., Leah, R., and Skriver, K., 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 (1997).
  • 37) Tronsmo, A., and Harman, G. E., Detection and quantification of N-acetyl-β-D-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels. Anal. Biochem., 208, 74-79 (1993).
  • 38) Roberts, W. K., and Selitrennikoff, C. P., Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol., 134, 169-176 (1988).
  • 39) Brameld, K. A., and Goddard, W. A., The role of enzyme distortion in the single displacement mechanism of family 19 chitinases. Proc. Natl. Acad. Sci. USA, 95, 4276-4281 (1998).
  • 40) Garcia-Casado, G., Collada, C., Allona, I., Casado, R., Pacios, L. F., Argoncillo, C., and Gomez, L., Site-directed mutagenesis of active site residues in a class I endochitinase from chestnut seeds. Glycobiology, 8, 1021-1028 (1998).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.