메뉴 건너뛰기




Volumn 16, Issue 10, 2003, Pages 876-883

Inhibition of plant-pathogenic fungi by the barley cystatin Hv-CPI (Gene Icy) is not associated with its cysteine-proteinase inhibitory properties

Author keywords

Antifungal activity; Site directed mutagenesis

Indexed keywords

BOTRYOTINIA FUCKELIANA; BOTRYTIS; BOTRYTIS CINEREA; COLLETOTRICHUM; COLLETOTRICHUM GRAMINICOLA; FUNGI; GLOMERELLA GRAMINICOLA; GRAMINICOLA; HORDEUM VULGARE SUBSP. VULGARE; PLECTOSPHAERELLA CUCUMERINA; TRICHODERMA; TRICHODERMA VIRIDE;

EID: 17344392459     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI.2003.16.10.876     Document Type: Article
Times cited : (67)

References (34)
  • 2
    • 0033516575 scopus 로고    scopus 로고
    • Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site
    • Alvarez-Fernandez, M., Barrett, A., Gerhartz, B., Dando, P. M., Ni, J., and Abrahamson, M. 1999. Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site. J. Biol. Chem. 274:19195-19203.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19195-19203
    • Alvarez-Fernandez, M.1    Barrett, A.2    Gerhartz, B.3    Dando, P.M.4    Ni, J.5    Abrahamson, M.6
  • 3
    • 0025964094 scopus 로고
    • Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members
    • Arai, S., Watanabe, H., Kondo, H., Emori, Y., and Abe, K. 1991. Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members. J. Biochem. 109:294-298.
    • (1991) J. Biochem. , vol.109 , pp. 294-298
    • Arai, S.1    Watanabe, H.2    Kondo, H.3    Emori, Y.4    Abe, K.5
  • 6
    • 0035096379 scopus 로고    scopus 로고
    • Transformation of white poplar (Populus alba L.) with a novel Arabidopsis thaliana cysteine proteinase inhibitor and analysis of insect pest resistance
    • Delledonne, M., Allegro, G., Belenghi B., Balestrazzi, A., Picco, F., Levine, A., Zelasco, S., Calligari P., and Confalonieri, M. 2001. Transformation of white poplar (Populus alba L.) with a novel Arabidopsis thaliana cysteine proteinase inhibitor and analysis of insect pest resistance. Mol. Breed. 7:35-42.
    • (2001) Mol. Breed. , vol.7 , pp. 35-42
    • Delledonne, M.1    Allegro, G.2    Belenghi, B.3    Balestrazzi, A.4    Picco, F.5    Levine, A.6    Zelasco, S.7    Calligari, P.8    Confalonieri, M.9
  • 9
    • 0037109006 scopus 로고    scopus 로고
    • Direct monitoring of extracellular protease activities in microbial cultures
    • Girard, C., and Michaud, D. 2002. Direct monitoring of extracellular protease activities in microbial cultures. Anal. Biochem. 308:38-391.
    • (2002) Anal. Biochem. , vol.308 , pp. 38-391
    • Girard, C.1    Michaud, D.2
  • 10
    • 0032787406 scopus 로고    scopus 로고
    • The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants
    • Gutierrez-Campos, R., Torres-Acosta, J., Saucedo-Arias, L. J., and Gomez-Lim, M. A. 1999. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Nature Biotechnol. 17:1223-1226.
    • (1999) Nature Biotechnol. , vol.17 , pp. 1223-1226
    • Gutierrez-Campos, R.1    Torres-Acosta, J.2    Saucedo-Arias, L.J.3    Gomez-Lim, M.A.4
  • 12
    • 0033570186 scopus 로고    scopus 로고
    • Pearl millet cysteine protease inhibitor. Evidence for the presence of two distinct sites responsible for anti-fungal and anti-feedant activities
    • Joshi, B. N., Sainani, M. N., Bastawade, K. B., Deshpande, V. V., Gupta, V. S., and Ranjekar, P. K. 1999. Pearl millet cysteine protease inhibitor. Evidence for the presence of two distinct sites responsible for anti-fungal and anti-feedant activities. Eur. J. Biochem. 265:556-563.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 556-563
    • Joshi, B.N.1    Sainani, M.N.2    Bastawade, K.B.3    Deshpande, V.V.4    Gupta, V.S.5    Ranjekar, P.K.6
  • 13
    • 0025160575 scopus 로고
    • Two distinct cystatins in rice with different specificities against proteinases
    • Kondo, H., Abe, K., Nishimura, I., Watanabe, H., Emori, Y., and Arai, S. 1990. Two distinct cystatins in rice with different specificities against proteinases. J. Biol. Chem. 265:15832-15837.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15832-15837
    • Kondo, H.1    Abe, K.2    Nishimura, I.3    Watanabe, H.4    Emori, Y.5    Arai, S.6
  • 14
    • 0030027738 scopus 로고    scopus 로고
    • Oryzacystatins exhibit growth inhibitory and lethal effects on different species of bean insect pests
    • Kuroda, M., Ishimoto, M., Suzuki, K., Kondo, H., Abe, K., Kitamura, K., and Arai S. 1996. Oryzacystatins exhibit growth inhibitory and lethal effects on different species of bean insect pests. Biosci. Biotechnol. Biochem. 60:209-212.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 209-212
    • Kuroda, M.1    Ishimoto, M.2    Suzuki, K.3    Kondo, H.4    Abe, K.5    Kitamura, K.6    Arai, S.7
  • 16
    • 0032211213 scopus 로고    scopus 로고
    • Structural and phylogenetic relationship among plant and animal cystatins
    • Margis, R., Reis, E. M., and Villeret, V. 1998. Structural and phylogenetic relationship among plant and animal cystatins. Arch. Biochem. Biophys. 359:24-30.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 24-30
    • Margis, R.1    Reis, E.M.2    Villeret, V.3
  • 17
    • 0032547704 scopus 로고    scopus 로고
    • Gel electrophoresis of proteolytic enzymes
    • Michaud, D. 1998. Gel electrophoresis of proteolytic enzymes. Anal. Chem. Acta 372:173-185.
    • (1998) Anal. Chem. Acta , vol.372 , pp. 173-185
    • Michaud, D.1
  • 18
    • 0034610303 scopus 로고    scopus 로고
    • Three-dimensional solution of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica
    • Nagata, K., Kudo, N., Abe, K., Arai, S., and Tanokura M. 2000. Three-dimensional solution of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry 39:14753-14760.
    • (2000) Biochemistry , vol.39 , pp. 14753-14760
    • Nagata, K.1    Kudo, N.2    Abe, K.3    Arai, S.4    Tanokura, M.5
  • 19
    • 0000316764 scopus 로고    scopus 로고
    • Characterization and distribution of chymotrypsin-like and other digestive proteases in Colorado potato beetle larvae
    • Novillo, C., Castañera, P., and Ortego, F. 1997. Characterization and distribution of chymotrypsin-like and other digestive proteases in Colorado potato beetle larvae. Arch. Insect Biochem. Physiol. 36:181-201.
    • (1997) Arch. Insect Biochem. Physiol. , vol.36 , pp. 181-201
    • Novillo, C.1    Castañera, P.2    Ortego, F.3
  • 20
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch, M. C. 1995. Protein modeling by E-mail. Biotechnology 13:658-660.
    • (1995) Biotechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 21
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modeling
    • Peitsch, M. C. 1996. ProMod and Swiss-Model: Internet-based tools for automated comparative protein modeling. Biochem. Soc. Trans. 224:274-279.
    • (1996) Biochem. Soc. Trans. , vol.224 , pp. 274-279
    • Peitsch, M.C.1
  • 22
    • 0037134658 scopus 로고    scopus 로고
    • Trypsin-like proteinases produced by Fusarium culmorum grown on grain proteins
    • Pekkarinen, A. I., and Jones B. L. 2002. Trypsin-like proteinases produced by Fusarium culmorum grown on grain proteins. J. Agric. Food Chem. 19:3849-3855.
    • (2002) J. Agric. Food Chem. , vol.19 , pp. 3849-3855
    • Pekkarinen, A.I.1    Jones, B.L.2
  • 24
    • 0032406093 scopus 로고    scopus 로고
    • A chestnut seed cystatin differentially effective against cysteine proteinase inhibitor from closely related pests
    • Pernas, M., Sanchez-Monge, R., Gomez, L., and Salcedo, G. 1998. A chestnut seed cystatin differentially effective against cysteine proteinase inhibitor from closely related pests. Plant Mol. Biol. 38:1235-1242.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 1235-1242
    • Pernas, M.1    Sanchez-Monge, R.2    Gomez, L.3    Salcedo, G.4
  • 28
    • 0036489618 scopus 로고    scopus 로고
    • 87 kDa tomato cystatin exhibits properties of a defence protein and forms crystals in prosytemin over-expressing transgenic plants
    • Siqueira-Junior, C. L., Fernandes, K. V. S., Machado, O. L. T., Cunha, M., Gomes, V. M., Moura, D., and Jacinto, T. 2002. 87 kDa tomato cystatin exhibits properties of a defence protein and forms crystals in prosytemin over-expressing transgenic plants. Plant Physiol. Biochem. 40:247-254.
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 247-254
    • Siqueira-Junior, C.L.1    Fernandes, K.V.S.2    Machado, O.L.T.3    Cunha, M.4    Gomes, V.M.5    Moura, D.6    Jacinto, T.7
  • 30
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and barley trypsin inhibitors
    • Terras, F. R. G., Schoofs, H. M. E., Thevissen, K., Osborn, R. W., Vanderleyden, J., Cammue, B. P. A., and Broekaert, W. F. 1993. Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and barley trypsin inhibitors. Plant Physiol. 103:1311-1319.
    • (1993) Plant Physiol. , vol.103 , pp. 1311-1319
    • Terras, F.R.G.1    Schoofs, H.M.E.2    Thevissen, K.3    Osborn, R.W.4    Vanderleyden, J.5    Cammue, B.P.A.6    Broekaert, W.F.7
  • 32
    • 0033117381 scopus 로고    scopus 로고
    • Transgenic Arabidopsis leaf tissue expressing a modified oryzacystatin shows resistance to the field Deroceras retuculatum (Mull)
    • Walker, A. J., Urwin, P. E., Atkinson, H. J., Brain, P., Glen, D. M., and Shewry, P. R. 1999. Transgenic Arabidopsis leaf tissue expressing a modified oryzacystatin shows resistance to the field Deroceras retuculatum (Mull). Transgenic Res. 8:95-103.
    • (1999) Transgenic Res. , vol.8 , pp. 95-103
    • Walker, A.J.1    Urwin, P.E.2    Atkinson, H.J.3    Brain, P.4    Glen, D.M.5    Shewry, P.R.6
  • 33
    • 0034762513 scopus 로고    scopus 로고
    • Isolation of a homodimeric lectin with antifungal and antiviral activities from red kidney bean (Phaseolus vulgaris) seeds
    • Ye, X. J., Ng, T. B., Tsang, P. W., and Wang, J. 2001. Isolation of a homodimeric lectin with antifungal and antiviral activities from red kidney bean (Phaseolus vulgaris) seeds. J. Protein Chem. 20:367-375.
    • (2001) J. Protein Chem. , vol.20 , pp. 367-375
    • Ye, X.J.1    Ng, T.B.2    Tsang, P.W.3    Wang, J.4
  • 34
    • 0030220996 scopus 로고    scopus 로고
    • Two wound-inducible soybean cysteine proteinases have greater insect digestive proteinase inhibitory activities than a constitutive homolog
    • Zhao, Y., Botella, M. A., Subramanian, L., Niu, X., Nielsen, S. S., Bressan, R. A., and Hasegawa, P. M. 1996. Two wound-inducible soybean cysteine proteinases have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol. 111:1299-1306.
    • (1996) Plant Physiol. , vol.111 , pp. 1299-1306
    • Zhao, Y.1    Botella, M.A.2    Subramanian, L.3    Niu, X.4    Nielsen, S.S.5    Bressan, R.A.6    Hasegawa, P.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.