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Volumn 76, Issue 9, 2010, Pages 2769-2777

Identification, characterization, and regulation of a novel antifungal chitosanase gene (cho) inanabaena spp.

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-FUNGAL; ANTI-FUNGAL ACTIVITY; ANTIFUNGAL EFFECT; CATALYTIC RESIDUE; CHITOSAN OLIGOSACCHARIDE; CHITOSANASE; CYANOBACTERIAL SPECIES; DARK PERIODS; GLYCOSIDE HYDROLASES; LIGHT CONDITIONS; LIMITING CONDITION; PAIRWISE ALIGNMENT; PROTEIN SEQUENCES; PUTATIVE SIGNAL PEPTIDE; REVERSE TRANSCRIPTION; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; SPECIFIC PRIMERS; STATIONARY PHASE;

EID: 77951532673     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02673-09     Document Type: Article
Times cited : (30)

References (43)
  • 2
  • 3
    • 0029622470 scopus 로고
    • Site-directed mutagenesis of evolutionary conserved carboxylic amino acids in the chitosanase from Streptomyces sp. N174 reveals two residues essential for catalysis
    • Boucher, I., T. Fukamizo, Y. Honda, G. E. Wilick, W. A. Neugebauer, and R. Brzezinski. 1995. Site-directed mutagenesis of evolutionary conserved carboxylic amino acids in the chitosanase from Streptomyces sp. N174 reveals two residues essential for catalysis. J. Biol. Chem. 270:31077-31082.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31077-31082
    • Boucher, I.1    Fukamizo, T.2    Honda, Y.3    Wilick, G.E.4    Neugebauer, W.A.5    Brzezinski, R.6
  • 5
    • 0028127691 scopus 로고
    • The toxins of cyanobacteria
    • Carmichael, W. W. 1994. The toxins of cyanobacteria. Sci. Am. 270:78-86.
    • (1994) Sci. Am. , vol.270 , pp. 78-86
    • Carmichael, W.W.1
  • 6
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G., and B. Henrissat. 1995. Structures and mechanisms of glycosyl hydrolases. Structure 3:853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 7
    • 0030266280 scopus 로고    scopus 로고
    • Chitinous component of the cell wall of Fusarium oxysporum, its structure deduced from chitosanase digestion
    • Fukamizo, T., Y. Honda, H. Toyoda, S. Ouchi, and S. Goto. 1996. Chitinous component of the cell wall of Fusarium oxysporum, its structure deduced from chitosanase digestion. Biosci. Biotechnol. Biochem. 60:1705-1708.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1705-1708
    • Fukamizo, T.1    Honda, Y.2    Toyoda, H.3    Ouchi, S.4    Goto, S.5
  • 8
    • 0025687767 scopus 로고
    • Chitosan production from Rhizopus oryzae mycelia
    • Hang, Y. D. 1990. Chitosan production from Rhizopus oryzae mycelia. Biotechnol. Lett. 12:911-912.
    • (1990) Biotechnol. Lett. , vol.12 , pp. 911-912
    • Hang, Y.D.1
  • 10
    • 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
  • 11
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • 11. 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
  • 12
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases [1]
    • 12. Henrissat, B., and A. Bairoch. 1996. Updating the sequence based classification of glycosyl hydrolases. Biochem. J. 316:695-696. (Pubitemid 26182174)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 13
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and G. Davies. 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 14
    • 77957227509 scopus 로고
    • Chemical analysis of microbial cells
    • J. R. Norris and D. W. Ribbons (ed.), Academic Press, New York, NY.
    • Herbert, D., P. J. Phipps, and R. E. Strange. 1971. Chemical analysis of microbial cells, p. 209-344. In J. R. Norris and D. W. Ribbons (ed.), Methods in microbiology. Academic Press, New York, NY.
    • (1971) Methods in Microbiology
    • Herbert, D.1    Phipps, P.J.2    Strange, R.E.3
  • 16
    • 0037177815 scopus 로고    scopus 로고
    • Biochemical and genetic properties of Paenibacillus glycosyl hydrolase having chitosanase activity and discoidin domain
    • Kimoto, H., H. Kusaoke, I. Yamamoto, Y. Fujii, T. Onodera, and A. Taketo. 2002. Biochemical and genetic properties of Paenibacillus glycosyl hydrolase having chitosanase activity and discoidin domain. J. Biol. Chem. 277:14695-14702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14695-14702
    • Kimoto, H.1    Kusaoke, H.2    Yamamoto, I.3    Fujii, Y.4    Onodera, T.5    Taketo, A.6
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0032519353 scopus 로고    scopus 로고
    • GeneMark.hmm: New solutions for gene finding
    • Lukashin, A. V., and M. Borodovsky. 1998. GeneMark.hmm: new solutions for gene finding. Nucleic Acids Res. 26:1107-1115.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1107-1115
    • Lukashin, A.V.1    Borodovsky, M.2
  • 21
    • 2442605484 scopus 로고    scopus 로고
    • In vitro suppression of mycelial growth of Fusarium oxysporum by extracellular chitosanase of Sphingobacterium multivorum and cloning of the chitosanase gene csnSM1
    • Matsuda, Y., Y. Iida, T. Shinogi, K. Kakutani, T. Nonomura, and H. Toyodai. 2001. In vitro suppression of mycelial growth of Fusarium oxysporum by extracellular chitosanase of Sphingobacterium multivorum and cloning of the chitosanase gene csnSM1. J. Gen. Plant Pathol. 67:318-324.
    • (2001) J. Gen. Plant Pathol. , vol.67 , pp. 318-324
    • Matsuda, Y.1    Iida, Y.2    Shinogi, T.3    Kakutani, K.4    Nonomura, T.5    Toyodai, H.6
  • 23
    • 0037561991 scopus 로고    scopus 로고
    • GenDB-an open source genome annotation system for prokaryote genomes
    • Meyer, F., A. Goesmann, and A. C. McHardy. 2003. GenDB-an open source genome annotation system for prokaryote genomes. Nucleic Acids Res. 31:2187-2195.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2187-2195
    • Meyer, F.1    Goesmann, A.2    McHardy, A.C.3
  • 24
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Ann. Chem. 31:426-428.
    • (1959) Ann. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 25
    • 65349111199 scopus 로고    scopus 로고
    • Genotypic and phenotypic diversity of Anabaena isolates from diverse rice agro-ecologies of India
    • Nayak, S., R. Prasanna, B. M. Prasanna, and D. B. Sahoo. 2009. Genotypic and phenotypic diversity of Anabaena isolates from diverse rice agro-ecologies of India. J. Basic Microbiol. 49:165-177.
    • (2009) J. Basic Microbiol. , vol.49 , pp. 165-177
    • Nayak, S.1    Prasanna, R.2    Prasanna, B.M.3    Sahoo, D.B.4
  • 26
    • 0005868646 scopus 로고    scopus 로고
    • Purification, characterization, and gene analysis of a chitosanase (ChoA) from Matsuebacter chitosanotabidus 3001
    • Park, J. K., K. Shimono, N. Ochiai, K. Shigeru, M. Kurita, Y. Ohta, K. Tanaka, H. Matsuda, and M. Kawamukai. 1999. Purification, characterization, and gene analysis of a chitosanase (ChoA) from Matsuebacter chitosanotabidus 3001. J. Bacteriol. 181:6642-6649.
    • (1999) J. Bacteriol. , vol.181 , pp. 6642-6649
    • Park, J.K.1    Shimono, K.2    Ochiai, N.3    Shigeru, K.4    Kurita, M.5    Ohta, Y.6    Tanaka, K.7    Matsuda, H.8    Kawamukai, M.9
  • 27
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29:e45.
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 28
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl, M. W., G. W. Horgan, and L. Dempfle. 2002. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 30:e36.
    • (2002) Nucleic Acids Res. , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 29
    • 0033736717 scopus 로고    scopus 로고
    • Bioactivity in free-living and symbiotic cyanobacteria of the genus Nostoc
    • Piccardi, R., A. Frosini, M. R. Tredici, and M. C. Margheri. 2000. Bioactivity in free-living and symbiotic cyanobacteria of the genus Nostoc. J. Appl. Phycol. 12:53-556.
    • (2000) J. Appl. Phycol. , vol.12 , pp. 53-556
    • Piccardi, R.1    Frosini, A.2    Tredici, M.R.3    Margheri, M.C.4
  • 30
    • 0036308660 scopus 로고    scopus 로고
    • Fungal chitosan production and its characterization
    • Pochanavanich, P., and W. Suntornusk. 2002. Fungal chitosan production and its characterization. Lett. Appl. Microbiol. 35:17-21.
    • (2002) Lett. Appl. Microbiol. , vol.35 , pp. 17-21
    • Pochanavanich, P.1    Suntornusk, W.2
  • 32
    • 0024202813 scopus 로고
    • Isolation and purification of cyanobacteria
    • Rippka, R. 1988. Isolation and purification of cyanobacteria. Methods Enzymol. 167:3-27.
    • (1988) Methods Enzymol. , vol.167 , pp. 3-27
    • Rippka, R.1
  • 34
    • 0029843191 scopus 로고    scopus 로고
    • Microalgal metabolites: A new perspective
    • Shimizu, Y. 1996. Microalgal metabolites: a new perspective. Annu. Rev. Microbiol. 50:431-465.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 431-465
    • Shimizu, Y.1
  • 36
    • 0036559807 scopus 로고    scopus 로고
    • Functional expression of chitinase and chitosanase and their effects on morphologies in the yeast Schizosaccharomyces pombe
    • Shimono, K., H. Matsuda, and M. Kawamukai. 2002. Functional expression of chitinase and chitosanase and their effects on morphologies in the yeast Schizosaccharomyces pombe. Biosci. Biotechnol. Biochem. 66:1143-1147.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1143-1147
    • Shimono, K.1    Matsuda, H.2    Kawamukai, M.3
  • 37
    • 0025082840 scopus 로고
    • Effects of light, temperature, nitrate, orthophosphate and bacteria on growth of and hepatotoxin production by Oscillatoria agardhii strains
    • Sivonen, K. 1990. Effects of light, temperature, nitrate, orthophosphate and bacteria on growth of and hepatotoxin production by Oscillatoria agardhii strains. Appl. Environ. Microbiol. 56:2658-2666.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2658-2666
    • Sivonen, K.1
  • 38
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue green algae (order: Chroococcales)
    • Stanier, R. Y., R. Kunisawa, M. Mandai, and G. Cohen-Bazire. 1971. Purification and properties of unicellular blue green algae (order: Chroococcales). Bacteriol. Rev. 35:171-305.
    • (1971) Bacteriol. Rev. , vol.35 , pp. 171-305
    • Stanier, R.Y.1    Kunisawa, R.2    Mandai, M.3    Cohen-Bazire, G.4
  • 39
    • 0040347098 scopus 로고
    • Amino acid contents in four samples of chitosan-glucan complexes
    • Velichkov, A., and N. Sotirov. 1990. Amino acid contents in four samples of chitosan-glucan complexes. Dokl. Bolg. Akad. Nauk. 43:69-71.
    • (1990) Dokl. Bolg. Akad. Nauk. , vol.43 , pp. 69-71
    • Velichkov, A.1    Sotirov, N.2
  • 40
    • 34548400782 scopus 로고    scopus 로고
    • Studies on culture age versus exometabolite production in batch cultures of the cyanobacterium Nostoc insulare
    • Volk, R. B. 2007. Studies on culture age versus exometabolite production in batch cultures of the cyanobacterium Nostoc insulare. J. Appl. Phycol. 19: 491-495.
    • (2007) J. Appl. Phycol. , vol.19 , pp. 491-495
    • Volk, R.B.1
  • 41
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase Al of Bacillus circulons WL-12 as essential residues for chitinase activity
    • Watanabe, T., K. Kobori, K. Miyashita, T. Fujii, H. Sakai, M. Uchida, and H. Tanaka. 1993. Identification of glutamic acid 204 and aspartic acid 200 in chitinase Al of Bacillus circulons WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268:18567-18572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 42
    • 0018311793 scopus 로고
    • Production and isolation of chitosan from Mucor rouxii
    • White, S. A., P. R. Farina, and I. Fulton. 1979. Production and isolation of chitosan from Mucor rouxii. Appl. Environ. Microbiol. 38:323-328.
    • (1979) Appl. Environ. Microbiol. , vol.38 , pp. 323-328
    • White, S.A.1    Farina, P.R.2    Fulton, I.3
  • 43
    • 25144524964 scopus 로고    scopus 로고
    • New chitosan degrading strains that produce chitosanases similar to ChoA of Mitsuaria chitosanitabida
    • Yun, C. S., D. Amakata, Y. Matsuo, H. Matsuda, and M. Kawamukai. 2005. New chitosan degrading strains that produce chitosanases similar to ChoA of Mitsuaria chitosanitabida. Appl. Environ. Microbiol. 71:5138-5144.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5138-5144
    • Yun, C.S.1    Amakata, D.2    Matsuo, Y.3    Matsuda, H.4    Kawamukai, M.5


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