메뉴 건너뛰기




Volumn 67, Issue 4, 2003, Pages 847-855

Family 19 Chitinase of Streptomyces griseus HUT6037 Increases Plant Resistance to the Fungal Disease

Author keywords

Antifungal activity; Disease resistance; Family 19 chitinase; Streptomyces griseus; Transgenic rice

Indexed keywords

ANTIFUNGAL AGENT; CHITINASE; CHITINASE C;

EID: 0041819552     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.847     Document Type: Article
Times cited : (59)

References (36)
  • 1
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A., New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 4
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. Seeds at 1.8 A resolution
    • Hart, P. J., Pfluger, H. D., Monzingo, A. F., Hollis, T., and Robertus, J. D., The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 A resolution. J. Mol. Biol., 248, 402-413 (1995).
    • (1995) J. Mol. Biol. , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 6
    • 0032584768 scopus 로고    scopus 로고
    • Substrate assistance in the mechanism of family 18 chitinases: Theoretical studies of potential intermediates and inhibitors
    • Brameld, K. A., Shrader, W. D., Imperiali, B., and Goddard III, W. A., Substrate assistance in the mechanism of family 18 chitinases: theoretical studies of potential intermediates and inhibitors. J. Mol. Biol., 280, 913-923 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 913-923
    • Brameld, K.A.1    Shrader, W.D.2    Imperiali, B.3    Goddard, W.A.4
  • 7
  • 9
    • 0342972186 scopus 로고
    • Comparison of some molecular, enzymatic and antifungal properties of chitinase from thorn-apple, tobacco and wheat
    • Broekaert, W. F., Parijs, J. V., Allen, A. K., and Peumans, W. J., Comparison of some molecular, enzymatic and antifungal properties of chitinase from thorn-apple, tobacco and wheat. Physiol. Mol. Plant Pathol., 33, 319-331 (1988).
    • (1988) Physiol. Mol. Plant Pathol. , vol.33 , pp. 319-331
    • Broekaert, W.F.1    Parijs, J.V.2    Allen, A.K.3    Peumans, W.J.4
  • 10
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with antifungal properties
    • Leah, R., Tommerup, H., Svendsen, I., and Mundy, J., Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J. Biol. Chem., 266, 1564-1573 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 11
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum, A., Mauch, F., Vogeli, U., and Boller, T., Plant chitinases are potent inhibitors of fungal growth. Nature, 324, 365-367 (1986).
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vogeli, U.3    Boller, T.4
  • 12
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts, W. K., and Selitrennikoff, C. P., Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol., 134, 169-176 (1988).
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 13
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli, B., Boller, T., and Neuhaus, J. M., The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol., 103, 221-226 (1993).
    • (1993) Plant Physiol. , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.M.3
  • 14
    • 0001679537 scopus 로고    scopus 로고
    • Enhanced resistance against a fungal pathogen Sphaerotheca humuli in transgenic strawberry expressing a rice chitinase gene
    • Asao, H., Nishizawa, Y., Arai, S., Sato, T., Hirai, M., Yoshida, K., Shinmyo, A., and Hibi, T., Enhanced resistance against a fungal pathogen Sphaerotheca humuli in transgenic strawberry expressing a rice chitinase gene. Plant Biotechnology, 14, 145-149 (1997).
    • (1997) Plant Biotechnology , vol.14 , pp. 145-149
    • Asao, H.1    Nishizawa, Y.2    Arai, S.3    Sato, T.4    Hirai, M.5    Yoshida, K.6    Shinmyo, A.7    Hibi, T.8
  • 16
    • 0031936818 scopus 로고    scopus 로고
    • Transgenic cucumber plants harboring a rice chitinase gene exhibit enhanced resistance to gray mold (Botrytis cinerea)
    • Tabei, Y., Kitade, S., Nishizawa, Y., Kikuchi, N., Kayano, T., Hibi, T., and Akutsu, K., Transgenic cucumber plants harboring a rice chitinase gene exhibit enhanced resistance to gray mold (Botrytis cinerea). Plant Cell Rep., 17, 159-164 (1998).
    • (1998) Plant Cell Rep. , vol.17 , pp. 159-164
    • Tabei, Y.1    Kitade, S.2    Nishizawa, Y.3    Kikuchi, N.4    Kayano, T.5    Hibi, T.6    Akutsu, K.7
  • 17
    • 0032875559 scopus 로고    scopus 로고
    • Enhanced resistance to blast (Magnaporthe grisea) in transgenic Japonica rice by constitutive expression of rice chitinase
    • 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).
    • (1999) Theor. Appl. Genet. , vol.99 , pp. 383-390
    • Nishizawa, Y.1    Nishio, Z.2    Nakazono, K.3    Soma, M.4    Nakajima, E.5    Ugaki, M.6    Hibi, T.7
  • 18
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT6037
    • Ohno, T., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M., and Watanabe, T., A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT6037. J. Bacteriol., 178, 5065-5070 (1996).
    • (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
  • 19
    • 0036562552 scopus 로고    scopus 로고
    • Functional analysis of the chitin-binding domain of a bacterial family 19 chitinase: Substrate-binding affinity and cis-dominant enhancement of antifungal function
    • Itoh, Y., Kawase, T., Nikaidou, N., Fukada, H., Mitsutomi, M., Watanabe, T., and Itoh, Y., Functional analysis of the chitin-binding domain of a bacterial family 19 chitinase: substrate-binding affinity and cis-dominant enhancement of antifungal function. Biosci. Biotechnol. Biochem., 66, 1084-1092 (2002).
    • (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
  • 21
    • 0027507719 scopus 로고
    • Sequence variation, differential expression and chromosomal location of rice chitinase genes
    • Nishizawa, Y., Kishimoto, N., Saito, A., and Hibi, T., Sequence variation, differential expression and chromosomal location of rice chitinase genes. Mol. Gen. Genet., 241, 1-10 (1993).
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 1-10
    • Nishizawa, Y.1    Kishimoto, N.2    Saito, A.3    Hibi, T.4
  • 22
    • 0008926503 scopus 로고    scopus 로고
    • Characterization of a novel type of class II chitinase from rice (Oryza sativa L): Comparison with a class I chitinase. Genetics, Biochemistry and Ecology of Cellulose Degradation
    • Trung, N. H., Park, S. M., Nishizawa, Y., Watanabe, T., Yamamoto, K., Sasaki, T., and Itoh, Y., Characterization of a novel type of class II chitinase from rice (Oryza sativa L): comparison with a class I chitinase. Genetics, Biochemistry and Ecology of Cellulose Degradation. Proceedings of MIE BIOFORUM 98, 720-728 (1999).
    • (1999) Proceedings of MIE BIOFORUM , vol.98 , pp. 720-728
    • Trung, N.H.1    Park, S.M.2    Nishizawa, Y.3    Watanabe, T.4    Yamamoto, K.5    Sasaki, T.6    Itoh, Y.7
  • 23
    • 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., 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, 18567-18572 (1993).
    • (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
  • 24
  • 26
    • 0031524467 scopus 로고    scopus 로고
    • Rapid and efficient Agrobacterium-mediated transformation in rice
    • Toki, S., Rapid and efficient Agrobacterium-mediated transformation in rice. Plant Mol. Biol. Rep., 15, 16-21 (1997).
    • (1997) Plant Mol. Biol. Rep. , vol.15 , pp. 16-21
    • Toki, S.1
  • 27
    • 0022917028 scopus 로고
    • The hypervirulence of Agrobacterium tumefaciens A281 is encoded in a region of pTi-Bo542 outside of T-DNA
    • Hood, E. E., Helmer, G. L., Fraley, R. T., and Chilton, M. D., The hypervirulence of Agrobacterium tumefaciens A281 is encoded in a region of pTi-Bo542 outside of T-DNA. J. Bacteriol., 168, 1291-1301 (1986).
    • (1986) J. Bacteriol. , vol.168 , pp. 1291-1301
    • Hood, E.E.1    Helmer, G.L.2    Fraley, R.T.3    Chilton, M.D.4
  • 28
    • 0028483231 scopus 로고
    • Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA
    • Hiei, Y., Ohta, S., Komari, T., and Kumashiro, T., Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. Plant J., 6, 271-282 (1994).
    • (1994) Plant J. , vol.6 , pp. 271-282
    • Hiei, Y.1    Ohta, S.2    Komari, T.3    Kumashiro, T.4
  • 29
    • 0019883721 scopus 로고
    • A convenient synthesis of glycolchitin, a substrate of lysozyme
    • Yamada, H., and Imoto, T., A convenient synthesis of glycolchitin, a substrate of lysozyme. Carbohydr. Res., 92, 160-162 (1981).
    • (1981) Carbohydr. Res. , vol.92 , pp. 160-162
    • Yamada, H.1    Imoto, T.2
  • 30
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T., and Yagishita, K., A simple activity measurement of lysozyme. Agric. Biol. Chem., 35, 1154-1156 (1971).
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 31
    • 0036007921 scopus 로고    scopus 로고
    • Mutation of a chitinase-like gene causes ectopic deposition of lignin, aberrant cell shapes, and over-production of ethylene
    • 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 over-production of ethylene. Plant Cell, 14, 165-179 (2002).
    • (2002) Plant Cell , vol.14 , pp. 165-179
    • Zhong, R.1    Kays, S.J.2    Schroeder, B.P.3    Ye, Z.H.4
  • 32
    • 9444272215 scopus 로고    scopus 로고
    • Three chitinase genes (ChiA, chiC and chiD) comprise the chitinase system of Bacillus circulans WL-12
    • Alam, M. M., Mizutani, T., Isono, M., Nikaidou, N., and Watanabe, T., Three chitinase genes (chiA, chiC and chiD) comprise the chitinase system of Bacillus circulans WL-12. J. Ferment. Bioeng., 82, 28-36 (1996).
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 28-36
    • Alam, M.M.1    Mizutani, T.2    Isono, M.3    Nikaidou, N.4    Watanabe, T.5
  • 33
    • 0033229842 scopus 로고    scopus 로고
    • The third chitinase gene (ChiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases
    • Suzuki, K., Taiyoji, M., Sugawara, N., Nikaidou, N., Henrissat, B., and Watanabe, T., The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem. J., 343, 587-596 (1999).
    • (1999) Biochem. J. , vol.343 , pp. 587-596
    • Suzuki, K.1    Taiyoji, M.2    Sugawara, N.3    Nikaidou, N.4    Henrissat, B.5    Watanabe, T.6
  • 34
    • 0036116360 scopus 로고    scopus 로고
    • Detailed analysis of rice chitinase gene expression in transgenic cucumber plants showing different levels of disease resistance to gray mold (Botrytis cinerea). Plant Science
    • Kishimoto, K., Nishizawa, Y., Tabei, Y., Hibi, T., Nakajima, M., and Akutsu, K., Detailed analysis of rice chitinase gene expression in transgenic cucumber plants showing different levels of disease resistance to gray mold (Botrytis cinerea). Plant Science, 162, 655-662 (2002).
    • (2002) Plant Science , pp. 655-662
    • Kishimoto, K.1    Nishizawa, Y.2    Tabei, Y.3    Hibi, T.4    Nakajima, M.5    Akutsu, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.