메뉴 건너뛰기




Volumn 110, Issue 1, 1996, Pages 147-154

The broad bean gene VfNOD32 encodes a nodulin with sequence similarities to chitinases that is homologous to (α/β)8-barrel-type seed proteins

Author keywords

[No Author keywords available]

Indexed keywords

PHASEOLUS (ANGIOSPERM); VICIA FABA;

EID: 0030064326     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.110.1.147     Document Type: Article
Times cited : (21)

References (61)
  • 2
    • 0026761188 scopus 로고
    • Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: Similarity to bacterial chitinases
    • Blaiseau P-L, Lafay J-F (1992) Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: similarity to bacterial chitinases. Gene 120: 243-248
    • (1992) Gene , vol.120 , pp. 243-248
    • Blaiseau, P.-L.1    Lafay, J.-F.2
  • 3
    • 0028033747 scopus 로고
    • A proposed structure for "family 18" chitinases - A possible function for narbonin
    • Coulson AFW (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.W.1
  • 4
    • 0028155327 scopus 로고
    • The Rubisco complex protein: A protein induced by fruit removal that forms a complex with ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Crafts-Brandner SJ, Salvucci ME (1994) The Rubisco complex protein: a protein induced by fruit removal that forms a complex with ribulose-1,5-bisphosphate carboxylase/oxygenase. Planta 194: 110-116
    • (1994) Planta , vol.194 , pp. 110-116
    • Crafts-Brandner, S.J.1    Salvucci, M.E.2
  • 5
    • 0000497141 scopus 로고
    • Fruit removal in soybean induces the formation of an insoluble form of ribulose-1,5-bisphosphate carboxylase/oxygenase in leaf extracts
    • Crafts-Brandner SJ, Salvucci ME, Egli DB (1991) Fruit removal in soybean induces the formation of an insoluble form of ribulose-1,5-bisphosphate carboxylase/oxygenase in leaf extracts. Planta 183: 300-306
    • (1991) Planta , vol.183 , pp. 300-306
    • Crafts-Brandner, S.J.1    Salvucci, M.E.2    Egli, D.B.3
  • 8
    • 0000477510 scopus 로고
    • Diversity of abundant mRNA sequences and patterns of protein synthesis in etiolated and greened pea seedlings
    • de Vries SC, Springer J, Wessels JGH (1982) Diversity of abundant mRNA sequences and patterns of protein synthesis in etiolated and greened pea seedlings. Planta 156: 129-135
    • (1982) Planta , vol.156 , pp. 129-135
    • De Vries, S.C.1    Springer, J.2    Wessels, J.G.H.3
  • 9
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber GK, Petsko GA (1990) The evolution of α/β barrel enzymes. Trend Biochem Sci 15: 228-234
    • (1990) Trend Biochem Sci , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 10
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg AP, Vogelstein B (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132: 6-13
    • (1983) Anal Biochem , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 11
    • 0026565262 scopus 로고
    • Transmission blocking antibodies recognize microfilarial chitinase in Brugian lymphatic filariasis
    • Fuhrman JA, Lane WS, Smith RF, Piessens WF, Perler FP (1992) Transmission blocking antibodies recognize microfilarial chitinase in Brugian lymphatic filariasis. Proc Natl Acad Sci USA 89: 1548-1552
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1548-1552
    • Fuhrman, J.A.1    Lane, W.S.2    Smith, R.F.3    Piessens, W.F.4    Perler, F.P.5
  • 12
    • 0027168279 scopus 로고
    • Multiple domain-structure in a chitinase gene (ChiC) of Streptomyces lividans
    • Fujii T, Miyashita K (1993) Multiple domain-structure in a chitinase gene (ChiC) of Streptomyces lividans. J Gen Microbiol 139: 677-686
    • (1993) J Gen Microbiol , vol.139 , pp. 677-686
    • Fujii, T.1    Miyashita, K.2
  • 13
    • 1842339409 scopus 로고
    • Synthesis of high specific activity cDNA
    • Gerard GF (1988) Synthesis of high specific activity cDNA. Focus 10: 12-13
    • (1988) Focus , vol.10 , pp. 12-13
    • Gerard, G.F.1
  • 14
    • 0025863881 scopus 로고
    • Characterization of the pea ENOD12B gene and expression analyses of the two ENOD12 genes in nodule, stem and flower tissue
    • Govers F, Harmsen H, Heidstra R, Michielsen P, Prins M, van Kammen A, Bisseling T (1991) Characterization of the pea ENOD12B gene and expression analyses of the two ENOD12 genes in nodule, stem and flower tissue. Mol Gen Genet 228: 160-166
    • (1991) Mol Gen Genet , vol.228 , pp. 160-166
    • Govers, F.1    Harmsen, H.2    Heidstra, R.3    Michielsen, P.4    Prins, M.5    Van Kammen, A.6    Bisseling, T.7
  • 16
    • 0024316572 scopus 로고
    • Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466
    • Harpster MH, Dunsmuir P (1989) Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466. Nucleic Acids Res 17: 5395
    • (1989) Nucleic Acids Res , vol.17 , pp. 5395
    • Harpster, M.H.1    Dunsmuir, P.2
  • 17
    • 0026750171 scopus 로고
    • A TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 Å resolution
    • Hennig M, Schlesier B, Dauter Z, Pfeffer S, Betzel C, Höhne WE, Wilson KS (1992) A TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 Å resolution. FEBS Lett 306: 80-84
    • (1992) FEBS Lett , vol.306 , pp. 80-84
    • Hennig, M.1    Schlesier, B.2    Dauter, Z.3    Pfeffer, S.4    Betzel, C.5    Höhne, W.E.6    Wilson, K.S.7
  • 19
    • 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
  • 20
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones JDG, Grady KL, Suslow TV, Bedbrook JR (1986) Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J 5: 467-473
    • (1986) EMBO J , vol.5 , pp. 467-473
    • Jones, J.D.G.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 21
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes
    • Joshi CP (1987) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucleic Acids Res 15: 6643-6653
    • (1987) Nucleic Acids Res , vol.15 , pp. 6643-6653
    • Joshi, C.P.1
  • 22
    • 0024382168 scopus 로고
    • Amino acid sequence of chitinase from Streptomyces erythraeus
    • Kamei K, Yamamura Y, Hara S, Ikenama T (1989) Amino acid sequence of chitinase from Streptomyces erythraeus. J Biochem 105: 979-985
    • (1989) J Biochem , vol.105 , pp. 979-985
    • Kamei, K.1    Yamamura, Y.2    Hara, S.3    Ikenama, T.4
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0024529940 scopus 로고
    • Structural principles of α/β barrel proteins: The packing of the interior of the sheet
    • Lesk AM, Branden CI, Chothia C (1989) Structural principles of α/β barrel proteins: the packing of the interior of the sheet. Proteins 5: 139-148
    • (1989) Proteins , vol.5 , pp. 139-148
    • Lesk, A.M.1    Branden, C.I.2    Chothia, C.3
  • 28
    • 0001104150 scopus 로고
    • Tissue print hybridization. A simple technique for detecting organ- and tissue-specific gene expression
    • McClure BA, Guilfoyle TJ (1989) Tissue print hybridization. A simple technique for detecting organ- and tissue-specific gene expression. Plant Mol Biol 12: 517-524
    • (1989) Plant Mol Biol , vol.12 , pp. 517-524
    • McClure, B.A.1    Guilfoyle, T.J.2
  • 32
    • 0029278125 scopus 로고
    • Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: CDNA, gene structure and developmentally regulated formation
    • Nong VH, Schlesier B, Bassüner R, Repik A, Horstmann C, Müntz K (1995) Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: cDNA, gene structure and developmentally regulated formation. Plant Mol Biol 28: 61-72
    • (1995) Plant Mol Biol , vol.28 , pp. 61-72
    • Nong, V.H.1    Schlesier, B.2    Bassüner, R.3    Repik, A.4    Horstmann, C.5    Müntz, K.6
  • 33
    • 0027664990 scopus 로고
    • A survey of transcripts expressed specifically in root nodules of broadbean (Vicia faba L.)
    • Perlick AM, Pühler A (1993) A survey of transcripts expressed specifically in root nodules of broadbean (Vicia faba L.). Plant Mol Biol 22: 957-970
    • (1993) Plant Mol Biol , vol.22 , pp. 957-970
    • Perlick, A.M.1    Pühler, A.2
  • 34
    • 0024763205 scopus 로고
    • Genes involved in lipopolysaccharide production and symbiosis are clustered on the chromosome of Rhizobium leguminosarum biovar viciae VF39
    • Priefer U (1989) Genes involved in lipopolysaccharide production and symbiosis are clustered on the chromosome of Rhizobium leguminosarum biovar viciae VF39. J Bacteriol 171: 6161-6168
    • (1989) J Bacteriol , vol.171 , pp. 6161-6168
    • Priefer, U.1
  • 35
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • Robbins PW, Overbeye K, Albright C, Benfield B, Pero J (1992) Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene 111: 69-76
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Overbeye, K.2    Albright, C.3    Benfield, B.4    Pero, J.5
  • 36
    • 0026772129 scopus 로고
    • Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity
    • Romaguera A, Menge U, Breves R, Diekmann H (1992) Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity. J Bacteriol 174: 3450-3454
    • (1992) J Bacteriol , vol.174 , pp. 3450-3454
    • Romaguera, A.1    Menge, U.2    Breves, R.3    Diekmann, H.4
  • 37
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • Rost B, Sander C (1993) Prediction of protein structure at better than 70% accuracy. J Mol Biol 232: 584-599
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 38
    • 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
  • 40
    • 0026030641 scopus 로고
    • Database of homology-derived structures and the structural meaning of sequence alignment
    • Sander C, Schneider R (1991) Database of homology-derived structures and the structural meaning of sequence alignment. Proteins 9: 56-68
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 43
    • 0008611216 scopus 로고
    • Studies on seed globulins from legumes. VII. Narbonin, a 2S globulin from Vicia narbonensis L.
    • Schlesier B, Manteuffel R, Rudolph A, Behlke J (1978) Studies on seed globulins from legumes. VII. Narbonin, a 2S globulin from Vicia narbonensis L. Biochem Physiol Pflanz 173: 420-428
    • (1978) Biochem Physiol Pflanz , vol.173 , pp. 420-428
    • Schlesier, B.1    Manteuffel, R.2    Rudolph, A.3    Behlke, J.4
  • 44
    • 0027139026 scopus 로고
    • Rhizobial lipo-oligosaccharide signals and their role in plant morphogenesis: Are analogous lipophilic chitin derivatives produced by the plant?
    • Spaink HP, Wijfjes AHM, van Vliet TB, Kijne JW, Lugtenberg BJJ (1993) Rhizobial lipo-oligosaccharide signals and their role in plant morphogenesis: are analogous lipophilic chitin derivatives produced by the plant? Aust J Plant Physiol 20: 381-392
    • (1993) Aust J Plant Physiol , vol.20 , pp. 381-392
    • Spaink, H.P.1    Wijfjes, A.H.M.2    Van Vliet, T.B.3    Kijne, J.W.4    Lugtenberg, B.J.J.5
  • 45
    • 0023045731 scopus 로고
    • The current status and portability of our sequence handling software
    • Staden R (1986) The current status and portability of our sequence handling software. Nucleic Acids Res 14: 217-231
    • (1986) Nucleic Acids Res , vol.14 , pp. 217-231
    • Staden, R.1
  • 47
    • 0028001965 scopus 로고
    • Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases
    • Staehelin C, Schultze M, Kondorosi E, Mellor RB, Boller T, Kondorosi A (1994) Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases. Plant J 5: 319-330
    • (1994) Plant J , vol.5 , pp. 319-330
    • Staehelin, C.1    Schultze, M.2    Kondorosi, E.3    Mellor, R.B.4    Boller, T.5    Kondorosi, A.6
  • 50
    • 0000499308 scopus 로고
    • Nodulin gene expression and ENOD2 localization in effective, nitrogen-fixing and ineffective, bacteria-free nodules of alfalfa
    • van de Wiel C, Norris JH, Bochenek B, Dickstein R, Bisseling T, Hirsch AM (1990a) Nodulin gene expression and ENOD2 localization in effective, nitrogen-fixing and ineffective, bacteria-free nodules of alfalfa. Plant Cell 2: 1009-1017
    • (1990) Plant Cell , vol.2 , pp. 1009-1017
    • Van De Wiel, C.1    Norris, J.H.2    Bochenek, B.3    Dickstein, R.4    Bisseling, T.5    Hirsch, A.M.6
  • 52
    • 0002658689 scopus 로고
    • Suggested nomenclature for plant genes involved in nodulation and symbiosis
    • van Kammen A (1984) Suggested nomenclature for plant genes involved in nodulation and symbiosis. Plant Mol Biol Rep 2: 43-45
    • (1984) Plant Mol Biol Rep , vol.2 , pp. 43-45
    • Van Kammen, A.1
  • 53
    • 0025324979 scopus 로고
    • Correlation between ultrastructural differentiation of bacteroids and nitrogen fixation in Alfalfa nodules
    • Vasse J, de Billy F, Camut S, Truchet G (1990) Correlation between ultrastructural differentiation of bacteroids and nitrogen fixation in Alfalfa nodules. J Bacteriol 172: 4295-4306
    • (1990) J Bacteriol , vol.172 , pp. 4295-4306
    • Vasse, J.1    De Billy, F.2    Camut, S.3    Truchet, G.4
  • 54
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne G (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14: 4683-4690
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 55
    • 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, 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: 18567-18572
    • (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
  • 56
    • 0026571181 scopus 로고
    • 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
    • Watanabe T, Oyanagi W, Suzuki K, Ohnishi K, 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
    • (1992) J Bacteriol , vol.174 , pp. 408-414
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Ohnishi, K.4    Tanaka, H.5
  • 57
    • 0025171327 scopus 로고
    • Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin
    • Watanabe T, Suzuki K, Oyanagi W, Ohnishi K, Tanaka H (1990) Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J Biol Chem 265: 15659-15665
    • (1990) J Biol Chem , vol.265 , pp. 15659-15665
    • Watanabe, T.1    Suzuki, K.2    Oyanagi, W.3    Ohnishi, K.4    Tanaka, H.5
  • 58
    • 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.