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Volumn 44, Issue 6, 1997, Pages 614-624

Structural and evolutionary relationships among chitinases of flowering plants

Author keywords

Angiosperms; Class I, II, III, and IV; Dicots; Endochitinase evolution; Monocots; Nuclear genes; PR proteins

Indexed keywords

CHITINASE;

EID: 0030909499     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006184     Document Type: Article
Times cited : (91)

References (61)
  • 1
    • 85007740421 scopus 로고
    • Structural classification of plant chitinases: Two subclasses in class I and class II chitinases
    • Araki T, Torikata T (1995) Structural classification of plant chitinases: two subclasses in class I and class II chitinases. Biosci Biotech Biochem 59:336-338
    • (1995) Biosci Biotech Biochem , vol.59 , pp. 336-338
    • Araki, T.1    Torikata, T.2
  • 2
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitin-binding proteins
    • Beintema JJ (1994) Structural features of plant chitinases and chitin-binding proteins. FEBS Lett 350:159-163
    • (1994) FEBS Lett , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 3
    • 0000358674 scopus 로고
    • Ethylene and the regulation of antifungal hydrolases in plants
    • Mitlin BJ (ed) Oxford University Press, Oxford
    • Boller T (1988) Ethylene and the regulation of antifungal hydrolases in plants. In: Mitlin BJ (ed) Surveys of plant molecular and cell biology, vol 5. Oxford University Press, Oxford, pp 145-174
    • (1988) Surveys of Plant Molecular and Cell Biology , vol.5 , pp. 145-174
    • Boller, T.1
  • 6
    • 0028033747 scopus 로고
    • A proposed structure for "family 18" chitinases. A possible function for narbonin
    • Coulson AF (1994) A proposed structure for "family 18" chitinases. A possible function for narbonin. FEBS Lett 354:41-44
    • (1994) FEBS Lett , vol.354 , pp. 41-44
    • Coulson, A.F.1
  • 7
    • 0027665777 scopus 로고
    • Molecular characterization of four chitinase cDNAs obtained from Cladosporium fulvum-infected tomato
    • Danhash N, Wagemakers CAM, van Kan JAL, de Wit PJGM (1993) Molecular characterization of four chitinase cDNAs obtained from Cladosporium fulvum-infected tomato. Plant Mol Biol 22:1017-1029
    • (1993) Plant Mol Biol , vol.22 , pp. 1017-1029
    • Danhash, N.1    Wagemakers, C.A.M.2    Van Kan, J.A.L.3    De Wit, P.J.G.M.4
  • 8
    • 0026245274 scopus 로고
    • Populus chitinase genes: Structure, organization, and similarity of translated sequences to herbaceous plant chitinases
    • Davis JM, Clarke HRG, Bradshaw HD Jr, Gordon MP (1991) Populus chitinase genes: structure, organization, and similarity of translated sequences to herbaceous plant chitinases. Plant Mol Biol 17:631-639
    • (1991) Plant Mol Biol , vol.17 , pp. 631-639
    • Davis, J.M.1    Clarke, H.R.G.2    Bradshaw Jr., H.D.3    Gordon, M.P.4
  • 10
    • 0023643145 scopus 로고
    • In vitro synthesis and processing of a bean pathogenesis-related (PR4) protein
    • De Tapia M, Dietrich A, Burkard G (1987) In vitro synthesis and processing of a bean pathogenesis-related (PR4) protein. Eur J Biochem 166:554-563
    • (1987) Eur J Biochem , vol.166 , pp. 554-563
    • De Tapia, M.1    Dietrich, A.2    Burkard, G.3
  • 11
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smities O (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-395
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smities, O.3
  • 14
    • 0027573317 scopus 로고
    • Nucleotide sequence of a Brassica napus endochitinase gene
    • Hamel F, Bellemare G (1993) Nucleotide sequence of a Brassica napus endochitinase gene. Plant Physiol 101:1403
    • (1993) Plant Physiol , vol.101 , pp. 1403
    • Hamel, F.1    Bellemare, G.2
  • 17
    • 0027471830 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution
    • Hart PJ, Pfluger HD, Monzingo AF, Hollis T, Robertus JD (1995) The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution. J Mol Biol 229:189-193
    • (1995) J Mol Biol , vol.229 , pp. 189-193
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 18
    • 0028845991 scopus 로고
    • Crystal structure of concanavalin B at 1.65 Å resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis
    • Hennig M, Jansonius JN, Terwisscha van Scheltinga AC, Dijkstra BW, Schlesier B (1995) Crystal structure of concanavalin B at 1.65 Å resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis. J Mol Biol 254:237-246
    • (1995) J Mol Biol , vol.254 , pp. 237-246
    • Hennig, M.1    Jansonius, J.N.2    Terwisscha Van Scheltinga, A.C.3    Dijkstra, B.W.4    Schlesier, B.5
  • 19
    • 0025654530 scopus 로고
    • Weak sequence homologies among chitinases detected by clustering analysis
    • Henrissat B (1990) Weak sequence homologies among chitinases detected by clustering analysis. Protein Seq Data Anal 3:523-526
    • (1990) Protein Seq Data Anal , vol.3 , pp. 523-526
    • Henrissat, B.1
  • 20
    • 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
  • 21
    • 0028268204 scopus 로고
    • Structural similarity of plant chitinase and lysozymes from animals and phages
    • Holm L, Sander C (1994) Structural similarity of plant chitinase and lysozymes from animals and phages. FEBS Lett 340:129-132
    • (1994) FEBS Lett , vol.340 , pp. 129-132
    • Holm, L.1    Sander, C.2
  • 22
    • 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, Neuhaus J-M (1993) 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) Plant Physiol , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 23
    • 0027347474 scopus 로고
    • Cloning of a complementary DNA that encodes an acidic chitinase which is induced by ethylene and expression of the corresponding gene
    • Ishige F, Mori H, Yamazaki K, Imaseki H (1993) Cloning of a complementary DNA that encodes an acidic chitinase which is induced by ethylene and expression of the corresponding gene. Plant Cell Physiol 34:103-111
    • (1993) Plant Cell Physiol , vol.34 , pp. 103-111
    • Ishige, F.1    Mori, H.2    Yamazaki, K.3    Imaseki, H.4
  • 24
    • 0029328434 scopus 로고
    • Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco
    • Jach C, Gornhardt B, Mundy J, Logemann J, Pinsdorf E, Leah R, Schell J, Maas C (1995) Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J 8:97-109
    • (1995) Plant J , vol.8 , pp. 97-109
    • Jach, C.1    Gornhardt, B.2    Mundy, J.3    Logemann, J.4    Pinsdorf, E.5    Leah, R.6    Schell, J.7    Maas, C.8
  • 25
    • 0025739769 scopus 로고
    • The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex
    • Jekel PA, Hartmann JBH, Beintema JJ (1991) The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. Eur J Biochem 200:123-130
    • (1991) Eur J Biochem , vol.200 , pp. 123-130
    • Jekel, P.A.1    Hartmann, J.B.H.2    Beintema, J.J.3
  • 26
    • 0019296687 scopus 로고
    • A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences
    • Kimura M (1980) A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences. J Mol Evol 16:111-120
    • (1980) J Mol Evol , vol.16 , pp. 111-120
    • Kimura, M.1
  • 27
    • 0027136629 scopus 로고
    • Tissue specificity and induction of class I, II and III chitinases in barley (Hordeum vulgare)
    • Kragh KM, Jacobsen S, Mikkelsen JD, Nielsen KA (1993) Tissue specificity and induction of class I, II and III chitinases in barley (Hordeum vulgare). Physiol Plant 89:490-498
    • (1993) Physiol Plant , vol.89 , pp. 490-498
    • Kragh, K.M.1    Jacobsen, S.2    Mikkelsen, J.D.3    Nielsen, K.A.4
  • 29
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda MJ, Robbins PW (1991) Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol Chem 266:19758-19767
    • (1991) J Biol Chem , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 30
    • 0026901010 scopus 로고
    • Acidic and basic class III chitinase mRNA accumulation in response to TMV infection of tobacco
    • Lawton K, Ward E, Payne G, Moyer M, Ryals J (1992) Acidic and basic class III chitinase mRNA accumulation in response to TMV infection of tobacco. Plant Mol Biol 19:735-743
    • (1992) Plant Mol Biol , vol.19 , pp. 735-743
    • Lawton, K.1    Ward, E.2    Payne, G.3    Moyer, M.4    Ryals, J.5
  • 31
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with antifungal properties
    • Leah R, Tommerup H, Svendsen I, Mundy J (1991) Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J Biol Chem 266:1564-1573
    • (1991) J Biol Chem , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 32
    • 0001480645 scopus 로고
    • Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases
    • Legrand M, Kauffmann S, Geoffroy P, Fritig B (1987) Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci USA 84: 6750-6754
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6750-6754
    • Legrand, M.1    Kauffmann, S.2    Geoffroy, P.3    Fritig, B.4
  • 33
    • 0026499523 scopus 로고
    • The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase
    • Lerner DR, Raikhel NV (1992) The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase. J Biol Chem 267:11085-11091
    • (1992) J Biol Chem , vol.267 , pp. 11085-11091
    • Lerner, D.R.1    Raikhel, N.V.2
  • 35
    • 0028913997 scopus 로고
    • Molecular cloning and characterization of chitinase genes from Candida albicans
    • McCreath KJ, Specht CA, Robbins PW (1995) Molecular cloning and characterization of chitinase genes from Candida albicans. Proc Natl Acad Sci USA 92:2544-2548
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2544-2548
    • McCreath, K.J.1    Specht, C.A.2    Robbins, P.W.3
  • 36
    • 0026212171 scopus 로고
    • Isolation of a complementary DNA encoding the bean PR4 chitinase: An acidic enzyme with an amino-terminus cysteine-rich domain
    • Margis-Pinheiro M, Metz-Boutigue MH, Awade A, de Tapia M, le Ret M, 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
    • (1991) Plant Mol Biol , vol.17 , pp. 243-253
    • Margis-Pinheiro, M.1    Metz-Boutigue, M.H.2    Awade, A.3    De Tapia, M.4    Le Ret, M.5    Burkard, G.6
  • 37
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves
    • Mauch F, Stahelin 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
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Stahelin, A.2
  • 38
    • 0001818585 scopus 로고
    • The primary structure of plant pathogenesis-related glucanohydrolases and their genes
    • Boller T, Meins F Jr (eds) Springer Verlag, New York
    • Meins F Jr, Neuhaus J-M, Sperisen C, Ryals J (1992) The primary structure of plant pathogenesis-related glucanohydrolases and their genes. In: Boller T, Meins F Jr (eds) Genes involved in plant defense. Springer Verlag, New York, pp 245-282
    • (1992) Genes Involved in Plant Defense , pp. 245-282
    • Meins Jr., F.1    Neuhaus, J.-M.2    Sperisen, C.3    Ryals, J.4
  • 42
    • 0030032332 scopus 로고    scopus 로고
    • Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eukaryotic families sharing a conserved core
    • Monzingo AF, Marcotte EM, Hart PJ, Robertus JD (1996) Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eukaryotic families sharing a conserved core. Nat Struct Biol 3: 133-140
    • (1996) Nat Struct Biol , vol.3 , pp. 133-140
    • Monzingo, A.F.1    Marcotte, E.M.2    Hart, P.J.3    Robertus, J.D.4
  • 43
    • 0022507362 scopus 로고
    • Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions
    • Nei M, Gojobori T (1986) Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol Biol Evol 3:418-426
    • (1986) Mol Biol Evol , vol.3 , pp. 418-426
    • Nei, M.1    Gojobori, T.2
  • 44
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole
    • Neuhaus J-M, Sticher L, Meins F Jr, Boller T (1991) 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
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10362-10366
    • Neuhaus, J.-M.1    Sticher, L.2    Meins Jr., F.3    Boller, T.4
  • 45
    • 0027631006 scopus 로고
    • An acidic class III chitinase in sugar beet: Induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants
    • Nielsen KK, Mikkelsen JD, Kragh KM, Bojsen K (1993) An acidic class III chitinase in sugar beet: induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants. Mol Plant Microbe Interact 6:495-506
    • (1993) Mol Plant Microbe Interact , vol.6 , pp. 495-506
    • Nielsen, K.K.1    Mikkelsen, J.D.2    Kragh, K.M.3    Bojsen, K.4
  • 46
    • 0027507719 scopus 로고
    • Sequence variation, differential expression and chromosomal location of rice chitinase genes
    • Nishizawa Y, Kishimoto N, Saito A, Hibi T (1993) Sequence variation, differential expression and chromosomal location of rice chitinase genes. Mol Gen Genet 214:1-10
    • (1993) Mol Gen Genet , vol.214 , pp. 1-10
    • Nishizawa, Y.1    Kishimoto, N.2    Saito, A.3    Hibi, T.4
  • 47
    • 0030064326 scopus 로고    scopus 로고
    • The broad bean gene VfNOD32 encodes a nodulin with sequence similarities to chitinases that is homologous to (alpha/beta)8-barrel-type seed proteins
    • Perlick AM, Fruhling M, Schroder G, Frosch SC, Puhler A (1996) The broad bean gene VfNOD32 encodes a nodulin with sequence similarities to chitinases that is homologous to (alpha/beta)8-barrel-type seed proteins. Plant Physiol 110:147-154
    • (1996) Plant Physiol , vol.110 , pp. 147-154
    • Perlick, A.M.1    Fruhling, M.2    Schroder, G.3    Frosch, S.C.4    Puhler, A.5
  • 49
    • 0026933301 scopus 로고
    • Cloning and characterization of a pathogen-induced chitinase in Brassica napus
    • Rasmussen U, Bojsen K, Collinge DB (1992) Cloning and characterization of a pathogen-induced chitinase in Brassica napus. Plant Mol Biol 20:277-287
    • (1992) Plant Mol Biol , vol.20 , pp. 277-287
    • Rasmussen, U.1    Bojsen, K.2    Collinge, D.B.3
  • 50
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 51
    • 0001695171 scopus 로고
    • Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana
    • Samac DA, Hironaka CM, Yallaly PE, Shah DM (1990) Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana. Plant Physiol 93:907-914
    • (1990) Plant Physiol , vol.93 , pp. 907-914
    • Samac, D.A.1    Hironaka, C.M.2    Yallaly, P.E.3    Shah, D.M.4
  • 52
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A, Mauch F, Vogeli U, Boller T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324:365-367
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vogeli, U.3    Boller, T.4
  • 53
    • 0025402915 scopus 로고
    • Structure of a tobacco endochitinase gene: Evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain
    • Shinshi H, Neuhaus J-M, Ryals J, Meins F Jr (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
    • (1990) Plant Mol Biol , vol.14 , pp. 357-368
    • Shinshi, H.1    Neuhaus, J.-M.2    Ryals, J.3    Meins Jr., F.4
  • 56
    • 0028774705 scopus 로고
    • Crystal structure of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW (1994) Crystal structure of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2:1181-1189
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha Van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 57
    • 0026507396 scopus 로고
    • The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin
    • van Buuren M, Neuhaus J-M, Shinshi H, Ryals J, Meins F Jr (1992) The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin. Mol Gen Genet 232:460-469
    • (1992) Mol Gen Genet , vol.232 , pp. 460-469
    • Van Buuren, M.1    Neuhaus, J.-M.2    Shinshi, H.3    Ryals, J.4    Meins Jr., F.5
  • 58
    • 0027226356 scopus 로고
    • Examination of the role of tyrosine-174 in the catalytic mechanism of the Arabidopsis thaliana chitinase: Comparison of variant chitinases generated by site-directed mutagenesis and expressed in insect cells using baculovirus vectors
    • Verburg JG, Rangwala SH, Samac DA, Luckow VA, Huynh QK (1993) Examination of the role of tyrosine-174 in the catalytic mechanism of the Arabidopsis thaliana chitinase: comparison of variant chitinases generated by site-directed mutagenesis and expressed in insect cells using baculovirus vectors. Arch Biochem Biophys 300:223-230
    • (1993) Arch Biochem Biophys , vol.300 , pp. 223-230
    • Verburg, J.G.1    Rangwala, S.H.2    Samac, D.A.3    Luckow, V.A.4    Huynh, Q.K.5
  • 59
    • 0027658064 scopus 로고
    • Cloning of a class III acidic chitinase from chickpea
    • Vogelsang R, Barz W (1993) Cloning of a class III acidic chitinase from chickpea. Plant Physiol 103:297-298
    • (1993) Plant Physiol , vol.103 , pp. 297-298
    • Vogelsang, R.1    Barz, W.2
  • 60
    • 0024712231 scopus 로고
    • Date of the monocot-dicot divergence estimated from chloroplast DNA sequence data
    • Wolfe KH, Gouy M, Yang Y-W, Sharp PM, Li W-H (1989) Date of the monocot-dicot divergence estimated from chloroplast DNA sequence data. Proc Natl Acad Sci USA 86:6201-6205
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6201-6205
    • Wolfe, K.H.1    Gouy, M.2    Yang, Y.-W.3    Sharp, P.M.4    Li, W.-H.5
  • 61
    • 0026539865 scopus 로고
    • Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes
    • Yanai K, Takaya N, Kojima N, Horiuchi H, Ohta A, Takagi M (1992) Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes. J Bacteriol 174:7398-7406
    • (1992) J Bacteriol , vol.174 , pp. 7398-7406
    • Yanai, K.1    Takaya, N.2    Kojima, N.3    Horiuchi, H.4    Ohta, A.5    Takagi, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.