Plant chitinases

植物 生物
作者
David B. Collinge,Karsten M. Kragh,Jørn Dalgaard Mikkelsen,Klaus K. Nielsen,Ulla Rasmussen,Knud Vad
出处
期刊:Plant Journal [Wiley]
卷期号:3 (1): 31-40 被引量:859
标识
DOI:10.1046/j.1365-313x.1993.t01-1-00999.x
摘要

The Plant JournalVolume 3, Issue 1 p. 31-40 Free Access Plant chitinases David B. Collinge, David B. Collinge Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, DenmarkSearch for more papers by this authorKarsten M. Kragh, Karsten M. Kragh Maribo Seed Biotechnology, Danisco A/S, Langebrogade 1, 1001 Copenhagen K, DenmarkSearch for more papers by this authorJørn D. Mikkelsen, Jørn D. Mikkelsen Maribo Seed Biotechnology, Danisco A/S, Langebrogade 1, 1001 Copenhagen K, DenmarkSearch for more papers by this authorKlaus K. Nielsen, Klaus K. Nielsen Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, Denmark Maribo Seed Biotechnology, Danisco A/S, Langebrogade 1, 1001 Copenhagen K, DenmarkSearch for more papers by this authorUlla Rasmussen, Ulla Rasmussen Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, Denmark Plant Biology Section, Environmental Science and Technology Department, Risø National Laboratory, P.O. Box 42, 4000 Roskilde, Denmark †Department of Botany, Stockholm University, 10 691-Stockholm, Sweden.Search for more papers by this authorKnud Vad1, Knud Vad1 Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, Denmark ‡Diabetes Research, Novo-Nordisk A/S, Novo Allé, 2880 Bagsværd, Denmark.Search for more papers by this author David B. Collinge, David B. Collinge Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, DenmarkSearch for more papers by this authorKarsten M. Kragh, Karsten M. Kragh Maribo Seed Biotechnology, Danisco A/S, Langebrogade 1, 1001 Copenhagen K, DenmarkSearch for more papers by this authorJørn D. Mikkelsen, Jørn D. Mikkelsen Maribo Seed Biotechnology, Danisco A/S, Langebrogade 1, 1001 Copenhagen K, DenmarkSearch for more papers by this authorKlaus K. Nielsen, Klaus K. Nielsen Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, Denmark Maribo Seed Biotechnology, Danisco A/S, Langebrogade 1, 1001 Copenhagen K, DenmarkSearch for more papers by this authorUlla Rasmussen, Ulla Rasmussen Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, Denmark Plant Biology Section, Environmental Science and Technology Department, Risø National Laboratory, P.O. Box 42, 4000 Roskilde, Denmark †Department of Botany, Stockholm University, 10 691-Stockholm, Sweden.Search for more papers by this authorKnud Vad1, Knud Vad1 Section for Plant Pathology, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, 1871 Frederiksberg C, Copenhagen, Denmark ‡Diabetes Research, Novo-Nordisk A/S, Novo Allé, 2880 Bagsværd, Denmark.Search for more papers by this author First published: January 1993 https://doi.org/10.1046/j.1365-313X.1993.t01-1-00999.xCitations: 622 *fax + 45 35 28 33 10 AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References Ary, M.B., Richardson, M. and Shewry, P.R. (1989) Purification and characterization of an insect α-amylase inhibitor/endochitinase from seeds of Job's tears (Coix lachryma-job). Biochim. Biophys. Acta, 993, 260– 266. Audy, P., Trudel, J. and Asselin, A. (1988) Purification and characterization of a lysozyme from wheat germ. Plant Sci. 58, 43– 50. Barber, M.S., Bertram, R.E. and Ride, J.P. (1989) Chitin oligosaccharides elicit lignification in wounded wheat leaves. Physiol. Mol. Plant Pathol. 34, 3– 12. Bartnicki-Garcia, S. (1968) Cell wall chemistry, morphogenesis, and taxonomy of fungi. Ann. Rev. Microbiol. 22, 87– 108. Benhamou, N. and Asselin, A. (1989) Attempted localization of a substrate for chitinases in plant cells reveals abundant N-acetyl-D-glucosamine residues in secondary walls. Biology Cell 67, 341– 350. Benhamou, N., Joosten, M.H.A.J. and de Wit, P.J.G.M. (1990) Subcellular localization of chitinase and of its potential substrate in tomato root tissues infected by Fusarium oxysporium f. sp. radicis-lycopersici. Plant Physiol. 92, 1108– 1120. Bernasconi, P., Locher, R., Pilet, P.E., Jollès, J. and Jollès, P. (1987) Purification and N-terminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquifolia cultured in vitro. Biochim. Biophys. Acta, 915, 254– 260. Bernier, J., Van Leemputten, E., Horisberger, M., Bush, D.A. and Jollès, P. (1971) The turnip lysozyme. FEBS Lett. 14, 100– 104. Bol, J.F., Linthorst, H.J. and Cornellssen, B.J. (1990) Plant pathogenesis-related proteins induced by virus infection. Ann. Rev. Phytopathol. 28, 113– 138. Boller, T. (1987) Hydrolytic enzymes in plant disease resistance. In Plant–Microbe Interactions, Molecular and Genetic Perspectives, Volume3 ( T. Koshuge and E.W. Nester, eds). New York : Macmillan, pp. 385– 411. Boller, T. (1988) Ethylene and the regulation of antifungal hydrolases in plants. In Surveys of Plant Molecular and Cell Biology, Volume5 ( B.J. Miflin, ed.). Oxford : Oxford University Press, pp. 145– 174. Boller, T. and Vögeli, U. (1984) Vacuolar localization of ethylene-induced chitinase in bean leaves. Plant Physiol. 74, 442– 444. Boller, T. and Métraux, J.P. (1988) Extracellular localization of chitinase in cucumber. Physiol. Mol. Plant Pathol. 33, 11– 16. Boller, T., Gehri, A., Mauch, F. and Vögeli, U. (1983) Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta, 157, 22– 31. Bowles, D.J. (1990) Defense-related proteins in higher plants. Ann. Rev. Biochem. 59, 873– 907. Bowles, D.J., Gurr, S.J., Scollan, C., Atkinson, H.J. and Hammond-Kosack, K.E. (1991) Local and systemic changes in plant gene expression following root infection by cyst nematodes. In Biochemistry and Molecular Biology of Plant-Pathogen Interactions ( C.J. Smith, ed.). Oxford : Clarendon Press, pp. 225– 236. Brederode, F.T., Linthorst, H.J.M. and Bol, J.F. (1991) Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding. Plant Mol. Biol. 17, 1117– 1125. Broekaert, W.F., Parijs, J.V., Allen, A.K. and Peumans, W.J. (1988) Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol. Mol. Plant Pathol. 33, 319– 331. Broekaert, W.F., Parijs, J.V., Leyns, F., Joos, H. and Peumans, W.J. (1989) A chitin-binding lectin from stinging nettle rhizomes with antifungal properties. Science, 245, 1100– 1102. Broglie, K.E., Gaynor, J.J. and Broglie, R.M. (1986) Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc. Natl Acad. Sci. USA, 83, 6820– 6824. Broglie, K.E., Biddle, P., Cressman, R. and Broglie, R. (1989) Functional analysis of DNA sequences responsible for ethylene regulation of a bean chitinase promotor in transgenic tobacco. Plant Cell, 1, 599– 607. Broglie, K., Chet, I., Holliday, M., Cressman, R., Biddle, P., Knowlton, S., Mauvais, C.J. and Broglie, R. (1991) Transgenic plants with enhanced resistance to the fungal pathogen Rhizoctonia solani. Science, 254, 1194– 1197. Chrispeels, M.J. and Raikel, N.V. (1991) Lectins, lectin genes, and their role in plant defence. Plant Cell, 3, 1– 9. Collinge, D.B. and Slusarenko, A.J. (1987). Review: Plant gene expression in response to pathogens. Plant Mol. Biol. 9, 389– 410. Conrads-Strauch, J., Dow, M., Milligan, D.E., Parra, R. and Daniels, M.J. (1990) Induction of hydrolytic enzymes in Brassica campestris in response to pathovars of Xanthomonas campestris. Plant Physiol. 93, 238– 243. Daugrois, J.H., Lafitte, C., Barthe, J.P. and Touze, A. (1990) Induction of β-1,3-glucanase and chitinase activity in compatible and incompatible interactions between Colletotrichum lindemuthianum and bean cultivars. J. Phytopath. 130, 225– 234. Davis, J.M., Clarke, H.R.G., Bradshaw, H.D. and Gordon, M.P. (1991) Populus chitinase genes: structure, organization, and similarity of translated sequences to herbaceous plant chitinases. Plant Mol. Biol. 17, 631– 639. Dixon, R.A. and Harrison, M. (1990). Activation, structure and organization of genes involved in microbial defence in plants. Adv. Genet. 28, 165– 234. Fink, W., Liefland, M. and Mendgen, K. (1988) Chitinases and β-1,3-glucanases in the apoplastic compartment of oat leaves (Avena sativa L.). Plant Physiol. 88, 270– 275. Fink, W., Liefland, M. and Mendgen, K. (1990) Comparison of various stress responses in oat in compatible and nonhost resistant interactions with rust fungi. Physiol. Mol. Plant Pathol. 37, 309– 321. Fisher, R.F. and Long, S.R. (1992) Rhizobium-plant signal exchange. Nature, 357, 655– 660. Flemming, T.M., McCarthy, D.A., White, R.F., Antoniw, J.F. and Mikkelsen, J.D. (1991) Induction and characterization of some of the pathogenesis-related proteins in sugar beet. Physiol. Mol. Plant Pathol. 39, 147– 160. Fukuda, Y., Ohme, M. and Shinshi, H. (1991) Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells. Plant Mol. Biol. 16, 1– 10. Gaynor, J.J. (1988) Primary structure of an endochitinase mRNA from Solanum tuberosum. Nucl. Acids Res. 16, 5210. Grosset, J., Meyer, Y., Chartier, Y., Kauffmann, S., Legrand, M. and Fritig, B. (1990) Tobacco mesophyll protoplasts synthesize 1,3-β-glucanase, chitinases, and "osmotins" during in vitro culture. Plant Physiol. 92, 520– 527. Hedrick, S.A., Bell, J.N., Boller, T. and Lamb, C.J. (1988) Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding, and infection. Plant Physiol. 86, 182– 186. Henrissat, B. (1990) Weak sequence homologies among chitinases detected by clustering analysis. Protein Seq. Data. Anal. 3, 523– 526. Herget, T., Schell, J. and Schreier, P.H. (1990) Elicitor-specific induction of one member of the chitinase gene family in Arachis hypogaea. Mol. Gen. Genet. 224, 469– 476. Huang, J.-K., Wen, L., Swegle, M., Tran, H.-C., Thin, T.H., Naylor, H.M., Muthukrishnan, S. and Reeck, G.R. (1991) Nucleotide sequence of a rice genomic clone that encodes a class I endochitinase. Plant Mol. Biol. 16, 479– 480. Irving, H.R. and Kuć, J.A. (1990) Local and systemic inductions of peroxidase, chitinase and resistance in cucumber plants by K2HPO4. Physiol. Mol. Plant Pathol. 37, 355– 366. Jacobsen, S., Mikkelsen, J.D. and Hejgaard, J. (1990) Characterization of two antifungal endochitinases from barley grain. Physiol. Plant. 79, 554– 562. Jacobsen, S., Hauschild, M.Z. and Rasmussen, U. (1992) Induction by chromium ions of chitinases and polyamines in barley (Hordeum vulgare L.) and rape (Brassica napus L. ssp. oleifera). Plant Sci. 84, 119– 128. Jones, J.D.G., Dean, C., Gidoni, D., Gilbert, D., Bonde-Nutter, D., Lee, R., Bedbrook, J. and Dunsmuir, P. (1988) Expression of bacterial chitinase protein in tobacco leaves using two photosynthetic gene promotors. Mol. Gen. Genet. 212, 536– 542. de Jong, A., Cordewener, J., Lo Schiavo, F., Terzi, M., Vandekerckhove, J., Van Kammen, A. and De Vries, S.C. (1992) A carrot somatic embryo mutant is rescued by chitinase. Plant Cell, 4, 425– 433. Joosten, M.H.A.J. and de Wit, P.J.G.M. (1989) Identification of several pathogenesis-related proteins in tomato leaves inoculated with Cladosporium fulvum (syn. Fulvia fulva) as 1,3-β-glucanases and chitinases. Plant Physiol. 89, 945– 951. Keefe, D., Hinz, U. and Meins, F. Jr (1990) The effect of ethylene on the cell-type-specific and intracellular localization of β-1,3-glucanase and chitinase in tobacco leaves. Planta, 182, 43– 51. Kombrink, E., Schröder, M. and Hahlbrock, K. (1988) Several "pathogenesis-related" proteins in potato are β-1,3-glucanases and chitinases. Proc. Natl Acad. Sci. USA, 85, 782– 786. Kragh, K.M., Jacobsen, S. and Mikkelsen, J.D. (1990) Induction, purification and characterization of barley leaf chitinases. Plant Sci. 71, 55– 68. Kragh, K.M., Jacobsen, S., Mikkelsen, J.D. and Nielsen, K.A. (1991) Purification and characterization of three chitinases and one β-1,3-glucanase accumulating in the medium of cell suspension cultures of barley (Hordeum vulgareL.). Plant Sci. 76, 65– 77. Kurosaki, F., Tashiro, N. and Nishl, A. (1988) Role of chitinase and chitin oligosaccharides in lignification response of cultured carrot cells treated with mycelial walls. Plant Cell Physiol. 29, 527– 531. Laflamme, D. and Roxby, R. (1989) Isolation and nucleotide sequence of cDNA clones encoding potato chitinase genes. Plant Mol. Biol. 13, 249– 250. Lawton, K., Ward E., Payne, G., Moyer, M. and Ryals, J. (1992) Acidic and basic class III chitinase mRNA accumulation in response to TMV infection of tobacco. Plant Mol. Biol. 19, 735– 743. Leah, R., Tommerup, H., Svendsen, I. and Mundy, J. (1991) Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J. Biol. Chem. 226, 1564– 1573. Lerouge, P., Roche, P., Faucher, C., Maillet, F., Truchet, G., Promé, J.C. and Dénarié, J. (1990) Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal. Nature, 344, 781– 784. Linthorst, H.J.M. (1991) Pathogenesis-related proteins of plants. Crit. Rev. Plant Sci. 10, 123– 150. Linthorst, H.J.M., van Loon, L.C., van Rossum, C.M.A., Mayer, A., Bol, J.F., van Roekel, J.S.C., Meulenhoff, E.J.S. and Cornelissen, B.J.C. (1990) Analysis of acidic and basic chitinases from tobacco and petunia and their constitutive expression in transgenic tobacco. Mol. Plant-Microbe Interactions, 3, 252– 258. Lotan, T. and Fluhr, R. (1990) Xylanase, a novel elicitor of pathogenesis-related proteins in tobacco, uses a non-ethylene pathway for induction. Plant Physiol. 93, 811– 817. Lotan, T., Ori, N. and Fluhr, R. (1989) Pathogenesis-related proteins are developmentally regulated in tobacco flowers. Plant Cell, 1, 881– 887. Lucas, J., Henschen, A., Lottspeich, F., Voegeli, U. and Boller, T. (1985) Amino-terminal sequence of ethylene-induced bean leaf chitinase reveals similarities to sugar-binding domains of wheat germ agglutinin. FEBS Lett. 193, 208– 210. Majeau, N., Trudel, J. and Asselin, A. (1990) Diversity of cucumber chitinase isoforms and characterization of one seed basic chitinase with lysozyme activity. Plant Sci. 68, 9– 16. Margis-Pinheiro, M., Metz-Boutigue, M.H., Awade, A., Tapia, De M., Ret, Le M. and Burkard, G. (1991) Isolation of a complementary DNA encoding the bean PR4 chitinase: an acidic enzyme with an amino-terminus cysteine-rich domain. Plant Mol. Biol. 17, 243– 253. Mauch, F. and Staehelin, L.A. (1989) Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cell, 1, 447– 457. Mauch, F., Hadwiger, L.A. and Boller, T. (1984) Ethylene: symptom, not signal for the induction of chitinase and β-1,3-glucanase in pea pods by pathogens and elicitors. Plant Physiol. 76, 607– 611. Mauch, F., Hadwiger, L.A. and Boller, T. (1988a) Antifungal hydrolases in pea tissue. I. Purification and characterization of two chitinases and two β-1,3-glucanases differentially regulated during development and in response to fungal infection. Plant Physiol. 87, 325– 333. Mauch, F., Mauch-Mani, B. and Boller, T. (1988b) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol. 88, 936– 942. Memelink, J., Linthorst, H.J.M., Schilperoot, R.A. and Hoge, J.H.C. (1990) Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns. Plant Mol. Biol. 14, 119– 126. Métraux, J.P. and Boller, T. (1986) Local and systemic induction of chitinase in cucumber plants in response to viral, bacterial and fungal infections. Physiol. Mol. Plant Pathol. 28, 161– 169. Métraux, J.P., Burkhart, W., Moyer, M., Dincher, S., Middlesteadt, W., Williams, S., Payne, G., Carnes, M. and Ryals, J. (1989) Isolation of a complementary DNA encoding a chitinase with structural homology to a bifunctional lysozyme/chitinase. Proc. Natl Acad. Sci. USA, 86, 896– 900. Mikkelsen, J.D., Berglund, L., Nielsen, K.K., Christiansen, H. and Bojsen, K. (1992) Structure of endochitinase genes from sugar beets. In Advances in Chitin and Chitosan ( C.J. Brine, P.A. Sandford and J.P. Zikakis, eds). Amsterdam : Elsevier, in press. Molano, J., Durán, A. and Cabib, E. (1977) A rapid and sensitive assay for chitinase using tritiated chitin. Anal. Biochem. 83, 648– 656. Molano, J., Polacheck, I., Durán, A. and Cabib, E. (1979) An endochitinase from wheat germ. J. Biol. Chem. 254, 4901– 4907. Nasser, W., De Tapia, M., Kaufmann, S., Montasser-Kouhsari, S. and Burkard, G. (1988) Identification and characterization of a maize pathogenesis-related proteins. Four maize PR proteins are chitinases. Plant Mol. Biol. 11, 529– 538. Nasser, W., De Tapia, M. and Burkard, G. (1990) Maize pathogenesis-related proteins: characterization and cellular distribution of 1,3-β-glucanases and chitinases induced by brown mosaic virus infection or mercuric chloride treatment. Physiol. Mol. Plant Pathol. 36, 1– 14. Neale, A.D., Wahleithner, J.A., Lund, M., Bonnett, H.T., Kelly, A., Meeks-Wagner, D.R., Peacock, W.J. and Dennis, E.S. (1990) Chitinase, β-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation. Plant Cell, 2, 673– 684. Neucere, J.N., Cleveland, T.E. and Dischinger, C. (1991) Existence of chitinase activity in mature corn kernels. J. Agric. Food Sci. 39, 1326– 1328. Neuhaus, J.-M., Ahl-Goy, P., Hinz, U., Flores, S. and Meins, F. (1991a) High-level expression of a tobacco chitinase gene in Nicotiana sylvestris. Susceptibility of transgenic plants to Cercospora nicotianae infection. Plant Mol. Biol. 16, 141– 151. Neuhaus, J.-M., Sticher, L., Meins, F., Jr and Boller, T. (1991b) A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc. Natl Acad. Sci. USA, 88, 10362– 10366. Nielsen, K.A. (1991) Establishment and biochemical characterization of embryogenic cell suspensions of barley (Hordeum vulgare L.) Analysis of extracellular proteins secreted by cells in culture. Ph.D. Thesis. Denmark : Aarhus University. Nishizawa, Y. and Hibi, T. (1991) Rice chitinase gene: cDNA cloning and stress-induced expression. Plant Sci. 76, 211– 218. O'Brien, M. and Colwell, R.R. (1987) A rapid test for chitinase activity that uses 4-methylumbelliferyl-N-acetyl-β-D-glucosaminide. Appl. Environ. Microbiol. 53, 1718– 1720. Ordentlich, A., Elad, T. and Chet, I. (1988) The role of chitinase of Serratia marcescens in biocontrol of Sclerotium rolfsii. Phytopathology, 78, 84– 88. Parsons, T.J., Bradshaw, H.D. and Gordon, M.P. (1989) Systemic accumulation of specific mRNAs in response to wounding in poplar trees. Proc. Natl Acad. Sci. USA, 86, 7895– 7899. Payne, G., Ahl, P., Moger, M., Harper, A., Beck, J., Meins, F. and Ryals, J. (1990) Isolation of complementary DNA clones encoding pathogenesis-related proteins P and Q two acidic chitinases from tobacco. Proc. Natl Acad. Sci. USA, 87, 98– 102. Pegg, G.F. and Young, D.H. (1982) Purification and characterization of chitinase enzymes from healthy and Verticillium alboatrum-infected tomato plants and from V. atrum. Physiol. Plant Pathol. 21, 389– 409. Rasmussen, U., Bojsen, K. and Collinge, D.B. (1992a) Cloning and characterization of a pathogen-induced chitinase in Brassica napus. Plant Mol. Biol. 20, 277– 287. Rasmussen, U., Giese, H. and Mikkelsen, J.D. (1992b) Induction and purification of chitinase in Brassica napus L. spp. Oleifera infected with Phoma lingam. Planta. 187, 328– 334. Roberts, W.K. and Selitrennikoff, C.P. (1988) Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol. 134, 169– 176. Roby, D. and Esquerré-Tugayé, M.T. (1987) Purification and some properties of chitinases from melon plants infected by Colletotrichum lagenarium. Carbohydr. Res. 165, 93– 104. Roby, D., Toppan, A. and Esquerré-Tugayé, M.T. (1985) Cell surfaces in plant–microorganism interactions. V. Elicitors of fungal and of plant origin trigger the synthesis of ethylene and of cell wall hydroxyproline-rich glycoprotein in plants. Plant Physiol. 77, 700– 704. Roby, D., Toppan, A. and Esquerré-Tugayé, M.T. (1986) Cell surfaces in plant–microorganism interactions. VI. Elicitors of ethylene from Colletotrichum lagenarium trigger chitinase activity in melon plants. Plant Physiol. 81, 228– 233. Roby, D., Gadelle, A. and Toppan, A. (1987) Chitin oligosaccharides as elicitors of chitinase activity in melon plants. Biochem. Biophys. Res. Commun. 143, 885– 892. Roby, D., Broglie, K., Cressman, R., Biddle, P., Chet, I. and Broglie, R. (1990) Activation of a bean chitinase promotor in transgenic tobacco plants by phytopathogenic fungi. Plant Cell, 2, 999– 1007. Roche, P., Lerouge, P., Ponthus, C. and Promé, J.C. (1991a) Structural determination of bacterial nodulation factors involved in the Rhizobium meliloti-alfafa symbiosis. J. Biol. Chem. 266, 10933– 10940. Roche, P., Debellé, F., Maillet, F., Lerouge, P., Faucher, C., Truchet, G., Dénarié, J. and Promé, J.C. (1991b) Molecular basis of symbiotic host specificity in Rhizobium meliloti: nodH and nodPQ genes encode the sulfation of lipooligosaccharide signals. Cell, 67, 1131– 1143. Samac, D.A. and Shah, D.M. (1991) Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promotor. Plant Cell, 3, 1063– 1072. Samac, D.A., Hironaka, C.M., Yallaly, P.E. and Shah, D.M. (1990) Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana. Plant Physiol. 93, 907– 914. Schlumbaum, A., Mauch, F., Vögeli, U. and Boller, T. (1986) Plant chitinases are potent inhibitors of fungal growth. Nature, 324, 365– 367. Shapira, R., Ordentlich, A., Chet, I. and Oppenheim, A.B. (1989) Control of plant diseases by chitinases expressed from cloned DNA in Escherichia coli. Phytopathology, 79, 1246– 1249. Shinshi, H., Mohnen, D. and Meins, F. (1987) Regulation of plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc. Natl Acad. Sci. USA, 84, 89– 93. Shinshi, H., Neuhaus, J.-M., Ryals, J. and Meins, F. (1990) Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol. Biol. 14, 357– 368. Spaink, H.P. (1992) Rhizobial lipo-oligosaccharides: answers and questions. Plant Mol. Biol. in press. Spaink, H.P., Sheeley, D.M., van Brussel, A.A.N., Glushka, J., York, W.S., Tak, T., Geiger, O., Kennedy, E.P., Reinhold, V.N. and Lugtenberg, B.J.J. (1991) A novel highly unsaturated fatty acid moity of lipo-oligosaccharide signals determines host specificity of Rhizobium. Nature, 354, 125– 130. Spaink, H.P., Aarts, A., Bloemberg, G.V., Folch, J., Geiger, O., Schlaman, H.R.M., Thomas-Oates, J.E., van Brussel, A.A.N., Van de Sande, K., Van Spronsen, P., Wijfjes, A.H.M. and Lugtenberg, B.J.J. (1992) Rhizobial lipo-oligosaccharide signals: Their biosynthesis and their role in the plant. In Advances in Molecular Genetics of Plant–Microbe Interactions. Volume 2 ( E. Nester, ed.), in press. Spanu, P., Boller, T., Ludwig, A., Wlemken, A., Faccio, A. and Bonfante-Fasolo, P. (1989) Chitinase in roots of mycorrhizal Allium porrum: regulation and localization. Planta, 177, 447– 455. Staehelin, C., Müller, J., Mellor, R.B., Wiemken, A. and Boller, T. (1992) Chitinase and peroxidase in effective (fix+) and ineffective (fix–) soybean nodules. Planta, 187, 295– 300. Stanford, A., Bevan, M. and Northcote, D. (1989) Differential expression within a family of novel wound-induced genes in potato. Mol. Gen. Genet. 215, 200– 208. Swegle, M., Huang, J.-K., Lee, G. and Muthukrishnan, S. (1989) Identification of an endochitinase cDNA clone from barley aleurone cells. Plant Mol. Biol. 12, 403– 412. Toyoda, H., Matsuda, Y., Yamaga, T., Ikeda, S., Morita, M., Tamai, T. and Ouchi, S. (1991) Suppression of the powdery mildew pathogen by chitinase microinjected into barley coleoptile epidermal cells. Plant Cell Rep. 10, 217– 220. Truchet, G., Roche, P., Lerouge, P., Vasse, J., Camut, S., de Billy, F., Promé, J.C. and Dénarié, J. (1991) Sulphated lipooligosaccharide signals of Rhizobium meliloti elicit root nodule organogenesis in alfafa. Nature, 351, 670– 673. Trudel, J. and Asselin, A. (1989) Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 178, 362– 366. Trudel, J., Audy, P. and Asselin, A. (1989) Electrophoretic forms of chitinase activity in Xanthi-nc tobacco, healthy and infected with tobacco mosaic virus. Mol. Plant–Microbe Interactions, 2, 315– 324. Tsukamoto, T., Koga, D., Ide, A., Ishibashi, T., Horino-Matsoshige, M., Yagashita, K. and Imoto, T. (1984) Purification and some properties of chitinases from yam, Dioscorea opposita Thumb. Agric. Biol. Chem. 48, 931– 939. Tuzun, S., Rao, M.N., Vögeli, U., Schardl, C.L. and Kuć, J. (1989) Induced systemic resistance to Blue Mold: Early induction and accumulation of β-1,3-glucanases, chitinases, and other pathogenesis-related proteins (b-proteins) in immunized tobacco. Phytopathol. 79, 979– 983. Usui, T., Hayashi, Y., Nanjo, F., Sakai, K. and Ishido, Y. (1987) Transglycosylation reaction of a chitinase purified from Nocardia orientalis. Biochim. Biophys. Acta, 923, 302– 309. Usui, T., Matsui, H. and Isobe, K. (1990) Enzymatic synthesis of useful chito-oligosaccharides utilizing transglycosylation by chitinolytic enzymes in a buffer containing ammonium sulfate. Carbohydr. Res. 203, 65– 77. Vad, K. (1991) Molecular studies of the interaction between pea and the pathogenic fungus Asochyta pisi. Ph.D. Thesis. Copenhagen : Royal Veterinary and Agricultural University. Vad, K., Mikkelsen, J.D. and Collinge, D.B. (1991) Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi. Planta, 184, 24– 29. Van Brussel, A.A.N., Bakhulzen, R., Van Spronsen, P.C., Spaink, H.P., Tak, T., Lugtenberg, B.J.J. and Keijne, J.W. (1992) Induction of pre-infection thread structures in the host plant by lipo-oligosaccharides of Rhizobium. Science, 257, 70– 72. Van Buuren, M., Neuhaus, J.M., Shinshi, H., Ryals, J. and Meins, F. (1992) The structure of regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin. Mol. Gen. Genet. 232, 460– 469. Verburg, J.G., Smith, C.E., Lisek, C.A. and Khai Huynh, Q. (1992) Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide. J. Biol. Chem. 267, 3886– 3893. Vigniotelli, A. (1991) Der Einfluss von Ethylen und Elizitoren auf die Chitinaseaktivität und symbiotische Stickstoff-Fixerung von Glycine max, Phaseolus vulgaris und Pisum sativum. Diploma thesis. Basel : University of Basel. Voisey, C.R. and Slusarenko, A.J. (1989) Chitinase mRNA and enzyme activity in Phaseolus vulgaris (L.) increase more rapidly in response to avirulent than to virulent cells of Pseudomonas syringae pv. phaseolicola. Physiol. Mol. Plant. Pathol. 35, 403– 412. Vögeli, U., Meins, F. and Boller, T. (1988) Co-ordinated regulation of chitinase and β-1,3-glucanase in bean leaves. Planta, 174, 364– 372. Vögeli-Lange, R., Hansen-Gehri, A., Boller, T. and Meins, F. (1988) Induction of the defence-related glucanohydrolases, β-1,3-glucanase and chitinase, by tobacco mosaic virus infection of tobacco leaves. Plant Sci. 54, 171– 176. Wadsworth, S.A. and Zikakis, J.P. (1984) Chitinase from soybean seeds: Purification and some properties of the enzyme system. J. Agric. Food Chem. 32, 1284– 1288. Wantanabe, T., Oyanagi, W., Suzuki, K., Ohnishi, K. and Tanaka, H. (1992) Structure of the gene encoding chitinase D of Bacillus circulans WL-12 and possible homology of the enzyme to other prokaryotic chitinases and class III plant chitinases. J. Bacteriol. 174, 408– 414. Ward, E.R., Uknes, S.J., Williams, S.C., Dincher, S.S., Wiederhold, D.L., Alexander, D.C., Ahl-Goy, P., Métraux, J.P. and Ryals, J.A. (1991) Coordinate gene activity in response to agents that induce systemic acquired resistance. Plant Cell, 3, 1085– 1094. Wessels, J.G.H. (1986) Cell wall synthesis in apical hyphal growth. Int. Rev. Cytology, 104, 37– 79. Wessels, J.G.H. (1988) A steady state model for apical wall growth in fungi. Acta Bot. Neerl. 37, 3– 16. Wessels, J.G.H. and Sietsma, J.H. (1981) Fungal cell walls: A survey. In Encyclopedia of Plant Physiology, New Series, Volume 13B, Plant Carbohydrates II ( W. Tanner and F.A. Loewus, eds). Berlin : Springer-Verlag, pp. 352– 394. Wirth, S.J. and Wolf, G.A. (1990) Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity. J. Microbiol. Methods, 12, 197– 205. Wright, C.S., Gavilanes, F. and Peterson, D.L. (1984) Primary structure of wheat germ agglutinin isolectin 2. Peptide order deduced from X-ray structure. Biochem. 23, 280– 287. Wubben, J.P., Joosten, M.H.A.J., Van Kan, J.A.L. and de Wit, P.J.G.M. (1992) Subcellular localization of plant chitinases and 1–3,-β-glucanases in Cladosporium fulvum (syn. Fulvia fulva)-infected tomato leaves. Physiol. Mol. Plant Pathol. in press. Yalpani, N., Silverman, P., Wilson, T.M.A., Kleer, D.A. and Raskin, I. (1991) Salicylic acid is a systemic signal and an inducer of pathogenesis-related proteins in virus-infected tobacco. Plant Cell, 3, 809– 818. Zhu, Q. and Lamb, C.J. (1991) Isolation and characterization of a rice gene encoding a basic chitinase. Mol. Gen. Genet. 226, 289– 296. Citing Literature Volume3, Issue1January 1993Pages 31-40 ReferencesRelatedInformation

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
大幅提高文件上传限制,最高150M (2024-4-1)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
航行天下完成签到 ,获得积分10
2秒前
咯咯咯完成签到 ,获得积分10
4秒前
没用的三轮完成签到,获得积分10
18秒前
young完成签到 ,获得积分10
19秒前
萧水白应助科研通管家采纳,获得10
20秒前
莫即完成签到 ,获得积分10
21秒前
优秀的尔风完成签到,获得积分10
27秒前
superspace完成签到 ,获得积分10
29秒前
blUe发布了新的文献求助20
31秒前
井小浩完成签到 ,获得积分10
33秒前
雪酪芋泥球完成签到 ,获得积分10
34秒前
35秒前
41秒前
宅心仁厚完成签到 ,获得积分10
42秒前
传奇3应助blUe采纳,获得10
46秒前
viahit完成签到 ,获得积分10
50秒前
dada完成签到 ,获得积分10
51秒前
1分钟前
六一儿童节完成签到 ,获得积分10
1分钟前
小蘑菇应助wangtinglk采纳,获得10
1分钟前
1分钟前
燕山堂完成签到 ,获得积分10
1分钟前
pfliu完成签到 ,获得积分10
1分钟前
齐天完成签到 ,获得积分10
1分钟前
mengmenglv完成签到 ,获得积分0
1分钟前
doctorbin完成签到 ,获得积分10
1分钟前
wangtinglk完成签到,获得积分10
1分钟前
JOY完成签到 ,获得积分10
1分钟前
2分钟前
blUe发布了新的文献求助10
2分钟前
krathhong完成签到 ,获得积分10
2分钟前
wangtinglk发布了新的文献求助20
2分钟前
isedu完成签到,获得积分10
2分钟前
2分钟前
如意的馒头完成签到 ,获得积分10
2分钟前
多托郭完成签到 ,获得积分10
2分钟前
MRJJJJ完成签到,获得积分10
2分钟前
2分钟前
dablack发布了新的文献求助10
2分钟前
2分钟前
高分求助中
Licensing Deals in Pharmaceuticals 2019-2024 3000
Effect of reactor temperature on FCC yield 2000
Very-high-order BVD Schemes Using β-variable THINC Method 1020
PraxisRatgeber: Mantiden: Faszinierende Lauerjäger 800
Mission to Mao: Us Intelligence and the Chinese Communists in World War II 600
MATLAB在传热学例题中的应用 500
Geochemistry, 2nd Edition 地球化学经典教科书第二版,不要epub版本 431
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 基因 遗传学 催化作用 物理化学 免疫学 量子力学 细胞生物学
热门帖子
关注 科研通微信公众号,转发送积分 3303307
求助须知:如何正确求助?哪些是违规求助? 2937611
关于积分的说明 8482682
捐赠科研通 2611546
什么是DOI,文献DOI怎么找? 1426022
科研通“疑难数据库(出版商)”最低求助积分说明 662524
邀请新用户注册赠送积分活动 647023