메뉴 건너뛰기




Volumn 50, Issue 6, 2004, Pages 451-454

Enhancement of the antifungal activity of Bacillus subtilis F29-3 by the chitinase encoded by Bacillus circulans chiA gene

Author keywords

Antifungal activity; Bacillus circulans; Bacillus subtilis; chiA

Indexed keywords

BACTERIA; BIOASSAY; CELL CULTURE; DNA; GENES;

EID: 3543139242     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/w04-027     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 0014243809 scopus 로고
    • Cell wall chemistry, morphogenesis, and taxonomy of fungi
    • Bartnicki-Garcia, S. 1969. Cell wall chemistry, morphogenesis, and taxonomy of fungi. Annu. Rev. Microbiol. 22: 87-108.
    • (1969) Annu. Rev. Microbiol. , vol.22 , pp. 87-108
    • Bartnicki-Garcia, S.1
  • 2
    • 0029116455 scopus 로고
    • Transposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis
    • Chen, C.L., Chang, L.K., Chang, Y.S., Liu, S.T., and Tschen, J.S.M. 1995. Transposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis. Mol. Gen. Genet. 248: 121-125.
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 121-125
    • Chen, C.L.1    Chang, L.K.2    Chang, Y.S.3    Liu, S.T.4    Tschen, J.S.M.5
  • 3
    • 0028989744 scopus 로고
    • Chitinolytic Enterobacter agglomerans antagonistic to fungal plant pathogens
    • Chernin, L., Ismailov, Z., Haran, S., and Chet, I. 1995. Chitinolytic Enterobacter agglomerans antagonistic to fungal plant pathogens. Appl. Environ. Microbiol. 61: 1720-1726.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1720-1726
    • Chernin, L.1    Ismailov, Z.2    Haran, S.3    Chet, I.4
  • 4
    • 0031038259 scopus 로고    scopus 로고
    • Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans
    • Chernin, L., De La Fuente, L., Sobolev, V., Haran, S., Vorgias, C.E., Oppenheim, A.B., and Chet, I. 1997. Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans. Appl. Environ. Microbiol. 63: 834-839.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 834-839
    • Chernin, L.1    De La Fuente, L.2    Sobolev, V.3    Haran, S.4    Vorgias, C.E.5    Oppenheim, A.B.6    Chet, I.7
  • 5
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • Cohen-Kupiec, R., and Chet, I. 1998. The molecular biology of chitin digestion. Curr. Opion. Biotechnol. 9: 270-277.
    • (1998) Curr. Opion. Biotechnol. , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 6
    • 0002301028 scopus 로고
    • Genetic analysis
    • Edited by C.R. Harwood and S.M. Cutting. John Wiley & Sons Ltd, Chichester, England
    • Cutting, S., and Vander Horn, P.B. 1990. Genetic analysis. In Molecular biological methods for Bacillus. Edited by C.R. Harwood and S.M. Cutting. John Wiley & Sons Ltd, Chichester, England, pp. 27-74.
    • (1990) Molecular Biological Methods for Bacillus , pp. 27-74
    • Cutting, S.1    Vander Horn, P.B.2
  • 7
    • 0001552797 scopus 로고
    • Techniques for inoculum production and inoculation of lily leaves with Botrytis elliptica
    • Doss, R.P., Chastagner, G.A., and Riley, K.I. 1984. Techniques for inoculum production and inoculation of lily leaves with Botrytis elliptica. Plant Dis. 68: 854-856.
    • (1984) Plant Dis. , vol.68 , pp. 854-856
    • Doss, R.P.1    Chastagner, G.A.2    Riley, K.I.3
  • 8
    • 0034077363 scopus 로고    scopus 로고
    • Introduction of the Serratia marcescens chiA gene into an endophytic Pseudomonas fluorescens for the control of phytopathogenic fungi
    • Downing, K.J., and Thomson, J.A. 2000. Introduction of the Serratia marcescens chiA gene into an endophytic Pseudomonas fluorescens for the control of phytopathogenic fungi. Can. J. Microbiol. 46: 363-369.
    • (2000) Can. J. Microbiol. , vol.46 , pp. 363-369
    • Downing, K.J.1    Thomson, J.A.2
  • 10
    • 0026709204 scopus 로고
    • What's new in chitinase research?
    • Flach, J., Pilet, P.E., and Jollès, P. 1992. What's new in chitinase research? Experientia, 48: 701-716.
    • (1992) Experientia , vol.48 , pp. 701-716
    • Flach, J.1    Pilet, P.E.2    Jollès, P.3
  • 11
    • 0003133857 scopus 로고
    • The ecology of chitin degradation
    • Edited by K.C. Marshall. Plenum Press, New York
    • Gooday, G.W. 1990. The ecology of chitin degradation. In Advances in microbial ecology, vol. 11. Edited by K.C. Marshall. Plenum Press, New York. pp. 387-430.
    • (1990) Advances in Microbial Ecology , vol.11 , pp. 387-430
    • Gooday, G.W.1
  • 12
    • 0019838194 scopus 로고
    • Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in Escherichia coli, Bacillus subtilis, and Bacillus licheniformis
    • Imanaka, T., Tanaka, T., Tsunekawa, H., and Aiba, S. 1981. Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in Escherichia coli, Bacillus subtilis, and Bacillus licheniformis. J. Bacteriol. 147: 776-786.
    • (1981) J. Bacteriol. , vol.147 , pp. 776-786
    • Imanaka, T.1    Tanaka, T.2    Tsunekawa, H.3    Aiba, S.4
  • 13
    • 0021825108 scopus 로고
    • New shuttle vectors for Escherichia coli and Bacillus subtilis. II. Plasmid pHY300PLK, a multipurpose cloning vector with a polylinker, derived from pHY460
    • Ishiwa, H., and Shibahara, H. 1985. New shuttle vectors for Escherichia coli and Bacillus subtilis. II. Plasmid pHY300PLK, a multipurpose cloning vector with a polylinker, derived from pHY460. Jpn. J. Genet. 60: 235-243.
    • (1985) Jpn. J. Genet. , vol.60 , pp. 235-243
    • Ishiwa, H.1    Shibahara, H.2
  • 14
    • 0018773834 scopus 로고
    • Lysis of the cell wall of yeast Phaffia rhodozyme by a lytic complex from Bacillus circulans WL-12
    • Johnson, E.A., Villa, T.G., Lewis, M.J., and Phaff, H.J. 1979. Lysis of the cell wall of yeast Phaffia rhodozyme by a lytic complex from Bacillus circulans WL-12. J. Appl. Biochem. 1: 273-282.
    • (1979) J. Appl. Biochem. , vol.1 , pp. 273-282
    • Johnson, E.A.1    Villa, T.G.2    Lewis, M.J.3    Phaff, H.J.4
  • 15
    • 0036195363 scopus 로고    scopus 로고
    • Characterization of a chitinase gene from Stenotrophomonas maltophilia strain 34S1 and its involvement in biological control
    • Kobayashi, D.Y., Reedy, R.M., Bick, J.A., and Oudemans, P.V. 2002. Characterization of a chitinase gene from Stenotrophomonas maltophilia strain 34S1 and its involvement in biological control. Appl. Environ. Microbiol. 68: 1047-1054.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1047-1054
    • Kobayashi, D.Y.1    Reedy, R.M.2    Bick, J.A.3    Oudemans, P.V.4
  • 16
    • 0027968247 scopus 로고
    • The chitinase encoding Tn7-based chiA gene endows Pseudomonas fluorescens with the capacity to control plant pathogens in soil
    • Koby, S., Schickler, H., Chet, I., and Oppenheim, A.B. 1994. The chitinase encoding Tn7-based chiA gene endows Pseudomonas fluorescens with the capacity to control plant pathogens in soil. Gene, 147: 81-83.
    • (1994) Gene , vol.147 , pp. 81-83
    • Koby, S.1    Schickler, H.2    Chet, I.3    Oppenheim, A.B.4
  • 17
    • 0002854086 scopus 로고
    • Antifungal effects of bacilysin and fengymycin from Bacillus subtilis F-29-3. A comparison with activities of other Bacillus antibiotics
    • Loeffler, W., Tschen, J.S.M., Vanittanakom, N., Kugler, M., Knorpp, E., Hsieh, T.F., and Wu, T.G. 1986. Antifungal effects of bacilysin and fengymycin from Bacillus subtilis F-29-3. A comparison with activities of other Bacillus antibiotics. J. Phytopathol. 115: 204-213.
    • (1986) J. Phytopathol. , vol.115 , pp. 204-213
    • Loeffler, W.1    Tschen, J.S.M.2    Vanittanakom, N.3    Kugler, M.4    Knorpp, E.5    Hsieh, T.F.6    Wu, T.G.7
  • 18
    • 0028324914 scopus 로고
    • Synergistic interaction between fungal cell wall degrading enzymes and different antifungal compounds enhances inhibition of spore germination
    • Lorito, M., Peterbauer, C., Hayes, C.K., and Harman, G.E. 1994. Synergistic interaction between fungal cell wall degrading enzymes and different antifungal compounds enhances inhibition of spore germination. Microbiology, 140: 623-629.
    • (1994) Microbiology , vol.140 , pp. 623-629
    • Lorito, M.1    Peterbauer, C.2    Hayes, C.K.3    Harman, G.E.4
  • 20
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and Beckwith, J. 1986. A genetic approach to analyzing membrane protein topology. Science, 233: 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 21
    • 0031685976 scopus 로고    scopus 로고
    • Secondary metabolite and endochitinase dependent antagonism toward plant pathogenic microfungi of Pseudomonas fluorescens isolates from sugar beet rhizosphere
    • Nielsen, M.N., Sørensen, J., Fels, J., and Pedersen, H.C. 1998. Secondary metabolite and endochitinase dependent antagonism toward plant pathogenic microfungi of Pseudomonas fluorescens isolates from sugar beet rhizosphere. Appl. Environ. Microbiol. 64: 3563-3569.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3563-3569
    • Nielsen, M.N.1    Sørensen, J.2    Fels, J.3    Pedersen, H.C.4
  • 22
    • 0030834003 scopus 로고    scopus 로고
    • Heterologous chitinase gene expression to improve plant defense against phytopathogenic fungi
    • Schickler, H., and Chet, I. 1997. Heterologous chitinase gene expression to improve plant defense against phytopathogenic fungi. J. Ind. Microbiol. Biotechnol. 19: 196-201.
    • (1997) J. Ind. Microbiol. Biotechnol. , vol.19 , pp. 196-201
    • Schickler, H.1    Chet, I.2
  • 23
    • 0000206650 scopus 로고
    • Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organisms and separation and purification of lytic enzymes
    • Tanaka, H., and Phaff, H.J. 1965. Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organisms and separation and purification of lytic enzymes. J. Bacteriol. 89: 1570-1580.
    • (1965) J. Bacteriol. , vol.89 , pp. 1570-1580
    • Tanaka, H.1    Phaff, H.J.2
  • 24
    • 85004415421 scopus 로고
    • Cell walls of Piricularia oryzae I. Selective enzymolysis of Piricularia oryzae walls by wall-lytic enzymes of Bacillus circulans WL-12
    • Tanaka, H., Ogasawara, N., Nakajima, T., and Tamari, K. 1970. Cell walls of Piricularia oryzae I. Selective enzymolysis of Piricularia oryzae walls by wall-lytic enzymes of Bacillus circulans WL-12. J. Gen. Appl. Microbiol. 16: 39-60.
    • (1970) J. Gen. Appl. Microbiol. , vol.16 , pp. 39-60
    • Tanaka, H.1    Ogasawara, N.2    Nakajima, T.3    Tamari, K.4
  • 25
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel, J., and Asselin, A. 1989. Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 178: 362-366.
    • (1989) Anal. Biochem. , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 26
    • 4544368295 scopus 로고
    • Control of Rhizoctonia solani by Bacillus subtilis
    • Tschen, J.S.M. 1987. Control of Rhizoctonia solani by Bacillus subtilis. Trans. Mycol. Soc. Jpn. 28: 483-493.
    • (1987) Trans. Mycol. Soc. Jpn. , vol.28 , pp. 483-493
    • Tschen, J.S.M.1
  • 27
    • 0022457256 scopus 로고
    • Fengycin-a novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3
    • Vanittanakom, N., Loeffler, W., Koch, U., and Jung, G. 1986. Fengycin-a novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3. J. Antibiot. 39: 888-901.
    • (1986) J. Antibiot. , vol.39 , pp. 888-901
    • Vanittanakom, N.1    Loeffler, W.2    Koch, U.3    Jung, G.4
  • 28
    • 0025314392 scopus 로고
    • Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe, T., Oyanagi, W., Suzuki, K., and Tanaka, H. 1990. Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J. Bacteriol. 172: 4017-4022.
    • (1990) J. Bacteriol. , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4
  • 29
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • 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: 18 567-18 572.
    • (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
  • 30
    • 0032858156 scopus 로고    scopus 로고
    • Purification and characterization of chitinase from Bacillus circulans No. 4.1
    • Wiwat, C., Siwayaprahm, P., and Bhumiratana, A. 1999. Purification and characterization of chitinase from Bacillus circulans No. 4.1. Curr. Microbiol. 39: 134-140.
    • (1999) Curr. Microbiol. , vol.39 , pp. 134-140
    • Wiwat, C.1    Siwayaprahm, P.2    Bhumiratana, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.