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Volumn 19, Issue 10, 2009, Pages 1169-1175

Analysis of the involvement of chitin-binding domain of ChiCW in antifungal activity, and engineering a novel chimeric chitinase with high enzyme and antifungal activities

Author keywords

Antifungal activity; Chitin binding domain; Chitinase; Hybrid enzyme; Protein engineering

Indexed keywords

CHITINASE; CHITINASE CHICW; FIBRONECTIN; UNCLASSIFIED DRUG;

EID: 70849098783     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0811.624     Document Type: Article
Times cited : (13)

References (24)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 3543091560 scopus 로고    scopus 로고
    • Two-step purification of Bacillus circulans chitinase A1 expressed in Escherichia coli periplasm
    • Chen, C. T., C. J. Huang, Y. H. Wang, and C. Y. Chen. 2004. Two-step purification of Bacillus circulans chitinase A1 expressed in Escherichia coli periplasm. Protein Expr. Purif. 37: 27-31.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 27-31
    • Chen, C.T.1    Huang, C.J.2    Wang, Y.H.3    Chen, C.Y.4
  • 4
    • 0028135314 scopus 로고
    • Cloning and characterization of a chitinase (CHIT42) cDNA from the mycoparasitic fungus Trichoderma harzianum
    • Garcia, I., J. M. Lora, J. De la Cruz, T. Benitez, A. Llobell, and J. A. Pintor-Toro. 1994. Cloning and characterization of a chitinase (CHIT42) cDNA from the mycoparasitic fungus Trichoderma harzianum. Curr. Genet. 27: 83-89.
    • (1994) Curr. Genet. , vol.27 , pp. 83-89
    • Garcia, I.1    Lora, J.M.2    De La Cruz, J.3    Benitez, T.4    Llobell, A.5    Pintor-Toro, J.A.6
  • 5
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166: 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 6
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280: 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 7
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and A. Bairoch. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293: 781-788. (Pubitemid 23244564)
    • (1993) Biochemical Journal , vol.293 , Issue.3 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 8
    • 11144238616 scopus 로고    scopus 로고
    • High-level expression and characterization of two chitinases, ChiCH and ChiCW, of Bacillus cereus 28-9 in Escherichia coli
    • Huang, C. J. and C. Y. Chen. 2005. High-level expression and characterization of two chitinases, ChiCH and ChiCW, of Bacillus cereus 28-9 in Escherichia coli. Biochem. Biophys. Res. Commun. 327: 8-17.
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 8-17
    • Huang, C.J.1    Chen, C.Y.2
  • 9
    • 21244486744 scopus 로고    scopus 로고
    • Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9
    • Huang, C. J., T. K. Wang, S. C. Chung, and C. Y. Chen. 2005. Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9. J. Biochem. Mol. Biol. 38: 82-88.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 82-88
    • Huang, C.J.1    Wang, T.K.2    Chung, S.C.3    Chen, C.Y.4
  • 10
    • 33846492949 scopus 로고    scopus 로고
    • Functions of the C-terminal region of chitinase ChiCW from Bacillus cereus 28-9 in substrate-binding and hydrolysis of chitin
    • Huang, C. J. and C. Y. Chen. 2006 Functions of the C-terminal region of chitinase ChiCW from Bacillus cereus 28-9 in substrate-binding and hydrolysis of chitin. J. Microbiol. Biotechnol. 16: 1897-1903.
    • (2006) J. Microbiol. Biotechnol. , vol.16 , pp. 1897-1903
    • Huang, C.J.1    Chen, C.Y.2
  • 11
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T. and K. Yogishita. 1971. A simple activity measurement of lysozyme. Agric. Biol. Chem. 35: 1154-1156.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yogishita, K.2
  • 12
    • 0036562552 scopus 로고    scopus 로고
    • Functional analysis of the chitinbinding domain of a family 19 chitinase from Streptomyces griseus HUT6037: Substrate-binding affinity and cis-dominant increase of antifungal function
    • Itoh, Y., T. Kawase, N. Nikaidou, H. Fukada, M. Mitsutomi, T. Watanabe, and Y. Itoh. 2002. Functional analysis of the chitinbinding domain of a family 19 chitinase from Streptomyces griseus HUT6037: Substrate-binding affinity and cis-dominant increase of antifungal function. Biosci. Biotechnol. Biochem. 66: 1084-1092.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1084-1092
    • Itoh, Y.1    Kawase, T.2    Nikaidou, N.3    Fukada, H.4    Mitsutomi, M.5    Watanabe, T.6    Itoh, Y.7
  • 13
    • 33749827454 scopus 로고    scopus 로고
    • Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C
    • Itoh, Y., J. Watanabe, H. Fukada, R. Mizuno, Y. Kezuka, T. Nonaka, and T. Watanabe. 2006. Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C. Appl. Microbiol. Biotechnol. 72: 1176-1184.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 1176-1184
    • Itoh, Y.1    Watanabe, J.2    Fukada, H.3    Mizuno, R.4    Kezuka, Y.5    Nonaka, T.6    Watanabe, T.7
  • 14
    • 0033051268 scopus 로고    scopus 로고
    • Increased antifungal activity of Trichoderma harzianum transformants that overexpress a 33-kDa chitinase
    • Limon, M. C., J. A. Pintor-Toro, and T. Benitez. 1999. Increased antifungal activity of Trichoderma harzianum transformants that overexpress a 33-kDa chitinase. Phytopathology 89: 254-261.
    • (1999) Phytopathology , vol.89 , pp. 254-261
    • Limon, M.C.1    Pintor-Toro, J.A.2    Benitez, T.3
  • 15
    • 0035917427 scopus 로고    scopus 로고
    • Addition of substrate-binding domains increases substratebinding capacity and specific activity of a chitinase from Trichoderma harzianum
    • Limon, M. C., E. Margolles-Clark, T. Benitez, and M. Penttila. 2001. Addition of substrate-binding domains increases substratebinding capacity and specific activity of a chitinase from Trichoderma harzianum. FEMS Microbiol. Lett. 198: 57-63.
    • (2001) FEMS Microbiol. Lett. , vol.198 , pp. 57-63
    • Limon, M.C.1    Margolles-Clark, E.2    Benitez, T.3    Penttila, M.4
  • 16
    • 3042520658 scopus 로고    scopus 로고
    • Increased antifungal and chitinase specific activities of Trichoderma harzianum CECT 2413 by addition of a cellulose binding domain
    • Limon, M. C., M. R. Chacon, R. Mejias, J. Delgado-Jarana, A. M. Rincon, A. C. Codon, and T. Benitez. 2004. Increased antifungal and chitinase specific activities of Trichoderma harzianum CECT 2413 by addition of a cellulose binding domain. Appl. Microbiol. Biotechnol. 64: 675-685.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 675-685
    • Limon, M.C.1    Chacon, M.R.2    Mejias, R.3    Delgado-Jarana, J.4    Rincon, A.M.5    Codon, A.C.6    Benitez, T.7
  • 17
    • 37049184497 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C. and J. Beckwith. 1986. A genetic approach to analyzing membrane protein topology. Science 233: 1403-1408. (Pubitemid 17169373)
    • (1986) Science , vol.233 , Issue.4771 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 18
    • 0030726362 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain
    • Morimoto, K., S. Karita, T. Kimura, K. Sakka, and K. Ohmiya. 1997. Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J. Bacteriol. 179: 7306-7314. (Pubitemid 27509967)
    • (1997) Journal of Bacteriology , vol.179 , Issue.23 , pp. 7306-7314
    • Morimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 20
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT6037
    • Ohno, T., S. Armand, T. Hata, N. Nikaidou, B. Henrissat, M. Mitsutomi, and T. Watanabe. 1996. A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT6037. J. Bacteriol. 178: 5065-5070.
    • (1996) J. Bacteriol. , vol.178 , pp. 5065-5070
    • Ohno, T.1    Armand, S.2    Hata, T.3    Nikaidou, N.4    Henrissat, B.5    Mitsutomi, M.6    Watanabe, T.7
  • 21
    • 0020694602 scopus 로고
    • Protein engineering
    • Ulmer, K. M. 1983. Protein engineering. Science 219: 666-671.
    • (1983) Science , vol.219 , pp. 666-671
    • Ulmer, K.M.1
  • 22
    • 0345411954 scopus 로고    scopus 로고
    • The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis
    • Wang, F. P., Q. Li, Y. Zhou, M. G. Li, and X. Xiao. 2003. The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis. Proteins 53: 908-916.
    • (2003) Proteins , vol.53 , pp. 908-916
    • Wang, F.P.1    Li, Q.2    Zhou, Y.3    Li, M.G.4    Xiao, X.5
  • 23
    • 0025171327 scopus 로고
    • Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin
    • Watanabe, T., K. Suzuki, W. Oyanagi, K. Ohnishi, and H. Tanaka. 1990. Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J. Biol. Chem. 265: 15659-15665.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15659-15665
    • Watanabe, T.1    Suzuki, K.2    Oyanagi, W.3    Ohnishi, K.4    Tanaka, H.5
  • 24
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe, T., Y. Ito, T. Yamada, M. Hashimoto, S. Sekine, and H. Tanaka. 1994. The roles of the C-terminal domain and type III domains of chitinase Al from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176: 4465-4472. (Pubitemid 24237947)
    • (1994) Journal of Bacteriology , vol.176 , Issue.15 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.