Gene cloning, expression, purification and characterization of rice (Oryza sativa L.) class II chitinase CHT11

Enzyme and Microbial Technology

Volumn 43, Issue 1, 2008, Pages 19-24

  Xayphakatsa, Kosonh ^a   Tsukiyama, Takuji ^a   Inouye, Kuniyo ^a   Okumoto, Yutaka ^a   Nakazaki, Testuya ^a   Tanisaka, Takatoshi ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Adenosine 5 triphosphate (ATP); Antifungal activity; Chitinase; Glutathione S transferase (GST) fusion protein

Indexed keywords

CELL CULTURE; ENZYME ACTIVITY; GROWTH KINETICS; PURIFICATION;

ANTIFUNGAL ACTIVITY; CHITINASE; GLUTATHIONE-S-TRANSFERASE (GST) FUSION PROTEIN;

PROTEINS;

BUFFER; CHITINASE; CLASS II CHITINASE CHT11; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN;

ANIMAL CELL; ANTIFUNGAL ACTIVITY; ARTICLE; CHT11 GENE; ENZYME ANALYSIS; ENZYME PURIFICATION; ESCHERICHIA COLI; FUNGAL STRAIN; FUNGUS GROWTH; FUNGUS HYPHAE; GENE EXPRESSION; GENE OVEREXPRESSION; GROWTH INHIBITION; MOLECULAR CLONING; NONHUMAN; PH; PROTEIN EXPRESSION; RICE; SUPERNATANT; TEMPERATURE; TIME; TRICHODERMA VIRIDE;

ESCHERICHIA COLI; ORYZA SATIVA; TRICHODERMA VIRIDE;

EID: 43949136888     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2008.03.012     Document Type: Article

References (43)

1. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280 (1991) 309-316
2. Neuhaus J.M. Plant chitinase (PR-3, PR-4, PR-8, PR-11). In: Datta S.K., and Muthukrishnan S. (Eds). Pathogenesis-related proteins in plants (1999), CRC Press, New York 77-105
3. Roberts W.K., and Selitrennikoff C.P. Plant and bacterial chitinases differ in antifungal activity. J Gene Microbiol 134 (1988) 169-176
4. Schlumbaum A., Mauch F., Vogeli U., and Boller T. Plant chitinases are potent inhibitors of fungal growth. Nature 324 (1986) 365-367
5. Sela-Buurlage M.B., Ponstein A.S., Bres-Vloemans S.A., Melchers L.S., van den Elzen P.J.M., and Cornelissen B.J.C. Only specific tobacco (Nicotiana tabacum) chitinases and β-1,3-glucanases exhibit antifungal activity. Plant Physiol 101 (1993) 857-863
6. Anand A., Lei Z., Sumner L.W., Mysore K.S., Arakane Y., Bockus W.W., et al. Apoplastic extracts from a transgenic wheat line exhibiting lesion-mimic phenotype have multiple pathogenesis-related proteins that are antifungal. Mol Plant Microbe Inter 17 (2004) 1306-1317
7. Broglie K., Chet I., Holliday M., Cressman R., Biddle P., Knowlton S., et al. Transgenic plants with enhanced resistance to the fungal pathogen Rhizoctonia solani. Science 254 (1991) 1194-1197
8. Zareie R., Melanson D.L., and Murphy P.J. Isolation of fungal cell wall degrading proteins from barley (Hordeum vulgare L.) leaves infected with Rhynchosporium secalis. Mol Plant Microbe Inter 15 (2002) 1031-1039
9. Ferreira R.B., Monteiro S., Freitas R., Santos C., Chen Zh.J., Batista L.M., et al. The role of plant defence proteins in fungal pathogenesis. Mol Plant Pathol 8 (2007) 677-700
10. Staehelin C., Schultze M., Kondorosi E., Mellor R.B., Boller Th., and Kondorosi A. Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases. Plant J 5 (1994) 319-330
11. De Jong A.J., Cordewener J., Schiavo F.L., Terzi M., Vandekerckhove J., Kammen A.V., et al. A carrot somatic embryo mutant is rescued by chitinase. Plant cell 4 (1992) 425-433
12. De Jong A.J., Hendriks T., Meijer E.A., Penning M., Schiavo F.L., Terzi M., et al. Transient reduction in secreted 32 kDa chitinase prevents some somatic embryogenesis in carrot (Daucus carota L.) variant ts 11. Dev Genet 16 (1995) 332-343
13. Kragh K.M., Hendricks T., De Jong A.J., Schiavo F.L., Bucherna N., Hojrup P., et al. Characterization of chitinase able to rescue somatic embryos of the temperature sensitive carrot variant ts 11. Plant Mol Biol 31 (1996) 631-645
14. Hong J.K., and Hwang B.K. Induction by pathogen, salt and drought of a basic class II chitinase mRNA and its in situ localization in pepper (Capsicum annuum). Physiologia Plantarum 114 (2002) 549-558
15. Nakazaki T., Tsukiyama T., Okumoto Y., Kageyama D., Naito K., Inouye K., et al. Distribution, structure, organ-specific expression, and phylogenic analysis of the pathogenesis-related protein-3 chitinase gene family in rice (Oryza sativa L.). Genome 49 (2006) 619-630
16. Murray M.G., and Thompson W.F. Rapid isolation of high molecular weight plant DNA. Nucleic Acid Res 8 (1980) 4321-4325
17. Laemmli U.K. Cleavage of structural Proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
18. Imoto T., and Yagashita K. A simple activity measurement of lysozyme. Agric Biol Chem 35 (1971) 1154-1156
19. Sherman M., and Goldberg A.L. Heat shock induced phophorylation of GroEL alter its binding and dissociation from unfolded proteins. J Biol Chem 50 (1994) 31479-31483
20. Parsell D.A., and Lindquist S. The function of heat-shock proteins stress tolerance: Degradation and reactivation of damaged proteins. Annu Rev Genet 27 (1993) 437-496
21. Kim J., Kim Y.M., Koo B.S., Chae Y.K., and Yoon M.Y. Production and proteolytic assay of lethal factor from Bacillus anthracis. Protein Exp Purif 30 (2003) 293-300
22. Yu S., Xia D., Luo Q., Cheng Y., Takano T., and Liu S. Purification and characterization of carbonic anhydrase of rice (Oryza sativa L.) expressed in Escherichia coli. Protein Exp Purif 52 (2007) 379-383
23. Schein C.H., and Noteborn M.H.M. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Biotechnology 6 (1988) 291-294
24. Shirano Y., and Shibata D. Low temperature cultivation of Escherichia coli carrying a rice lipoxygenase L-2 cDNA produces a soluble and active enzyme at high level. FEBS Lett 181 (1990) 271-274
25. Steczko J., Donoho G.A., Dixon J.E., Sugimoto T., and Axelrod B. Effect of Ethanol and low-temperature culture on expression of soybean lipoxygenase L-1 in Escherichia coli. Protein Exp Purif 2 (1991) 221-227
26. Li Zh, Xiong F., Lin Q., Anjou M., Daugulis A.J., Yang D.S.C., et al. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Exp Purif 21 (2001) 438-445
27. Vera A., Gonzalez Montalban N., Aris A., and Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol Bioeng 96 (2007) 1101-1106
28. Scharnagl C., Reif M., and Friedrich J. Stability of protein: temperature, pressure and the role of the solvent. Biochim Biophys Acta 1749 (2005) 187-213
29. Wall J.G., and Pluckthun A. Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli. Curr Biotechnol 6 (1995) 507-516
30. Taira T., Toma N., Ichi M., Takeuchi M., and Ishihara M. Tissue distribution, synthesis stage, and ethylene induction of pineapple (Ananas comosus) chitinase. Biosci Biotechnol Biochem 69 (2005) 852-854
31. Iseli B., Boller T., and Neuhaus J.M. The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin biding but not for catalytic or antifungal activity. Plant Physiol 103 (1993) 221-226
32. Muta Y., Oneda H., and Inouye K. Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues. Biochem J 386 (2005) 263-270
33. Lee S., Mouri Y., Minoda M., Oneda H., and Inouye K. Comparison of the wild-type α-amylase and its variant enzymes of Bacillus amyloliquefaciens in their activity and thermal stability, and insights into engineering the thermal stability of Bacillus α-amyklase. J Biochem 139 (2006) 1007-1015
34. Lee S., Oneda H., Minoda M., Tanaka A., and Inouye K. Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis α-amylase and insights into engineering α-amylase variants active at acidic conditions. J Biochem 139 (2006) 997-1005
35. Andersen 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 (1997) 815-822
36. Yamagumi T., and Funatsu G. Limited proteolysis and reduction carboxymethylation of rye seed chitinase-a: role of the chitin binding domain in its chitinase action. Biosci Biotech Biochem 60 7 (1996) 1081-1086
37. Mauch F., and Staehelin A. Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant cell 1 (1989) 447-457
38. Taira T., Ohnuma T., Yamagami T., Aso Y., Ishiguro M., and Ishihara M. Antifungal activity of rye (Secale cereale) seed chitinase: the different binding manner of class I and class II chitinases to the fungal cell walls. Biosci Biotechnol Biochem 66 (2002) 970-977
39. Leung J., and Giraudat J. Abscisic acid signal transduction. Annu Rev Plant Physiol Plant Mol Biol 49 (1998) 199-222
40. Finkelstein R.R., Gampala S.S.L., and Rock C.D. Abscisic acid signaling in seeds and seedlings. Plant Cell 14 (2002) S15-S45
41. Xiong L., Schumaker K.S., and Zhu J.K. Cell signaling during cold, drought, and salt stress. Plant Cell 14 (2002) S165-S183
42. Zhu J.K. Salt and drought stress signal transduction in plants. Annu Rev Plant Biol 53 (2002) 247-273
43. Chen C.W., Yang Y.W., Lur H.S., Tsai Y.G., and Chang M.C. A novel function of abscisic acid in the regulation of rice (Oryza sativa L.) root growth and development. Plant Cell Physiol 47 (2006) 1-13