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Volumn 119, Issue 4, 1999, Pages 1547-1556

A gene encoding a hevein-like protein from elderberry fruits is homologous to PR-4 and class V chitinase genes

Author keywords

[No Author keywords available]

Indexed keywords

CHITIN BINDING PROTEIN; CLONING; HOMOLOGOUS RECOMBINATION; PLANT PRODUCT; PROTEIN EXPRESSION; PROTEIN ISOLATION;

EID: 0033117527     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.119.4.1547     Document Type: Article
Times cited : (47)

References (53)
  • 1
    • 0030293126 scopus 로고    scopus 로고
    • Potato lectin: A three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin
    • Allen AK, Bolwell GP, Brown DS, Sidebottom C, Slabas AR (1996) Potato lectin: a three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin. Int J Biochem Cell Biol 28: 1285-1291
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 1285-1291
    • Allen, A.K.1    Bolwell, G.P.2    Brown, D.S.3    Sidebottom, C.4    Slabas, A.R.5
  • 2
    • 0027510717 scopus 로고
    • Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif
    • Andersen NH, Cao B, Rodriguez-Romero A, Arreguin B (1993) Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif. Biochemistry 32: 1407-1422
    • (1993) Biochemistry , vol.32 , pp. 1407-1422
    • Andersen, N.H.1    Cao, B.2    Rodriguez-Romero, A.3    Arreguin, B.4
  • 3
    • 0029013978 scopus 로고
    • The interaction of hevein with n-acetyl-glucosamine-containing oligosaccharides: Solution structure of hevein complexed to chitobiose
    • Asensio JL, Cañada FJ, Bruix M, Rodriguez-Romero A, Jimenez-Barbero J (1995) The interaction of hevein with N-acetyl-glucosamine-containing oligosaccharides: solution structure of hevein complexed to chitobiose. Eur J Biochem 230: 621-633
    • (1995) Eur J Biochem , vol.230 , pp. 621-633
    • Asensio, J.L.1    Cañada, F.J.2    Bruix, M.3    Rodriguez-Romero, A.4    Jimenez-Barbero, J.5
  • 4
    • 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
  • 5
    • 0026556040 scopus 로고
    • The primary structure of stinging nettle (Urtica dioica) agglutinin: A two-domain member of the hevein family
    • Beintema JJ, Peumans WJ (1992) The primary structure of stinging nettle (Urtica dioica) agglutinin: a two-domain member of the hevein family. FEBS Lett 299: 131-134
    • (1992) FEBS Lett , vol.299 , pp. 131-134
    • Beintema, J.J.1    Peumans, W.J.2
  • 6
    • 11944249594 scopus 로고
    • Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis)
    • Broekaert WF, Lee H-I, Kush A, Chua N-H, Raikhel NV (1990) Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis). Proc Natl Acad Sci USA 87: 7633-7637
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7633-7637
    • Broekaert, W.F.1    Lee, H.-I.2    Kush, A.3    Chua, N.-H.4    Raikhel, N.V.5
  • 10
    • 0031413688 scopus 로고    scopus 로고
    • Temporal and spatial expression of mRNAs encoding pathogenesis-related proteins during ethylene-promoted leaflet abscission in sambucus nigra
    • Coupe SA, Taylor JE, Roberts JA (1997) Temporal and spatial expression of mRNAs encoding pathogenesis-related proteins during ethylene-promoted leaflet abscission in Sambucus nigra. Plant Cell Environ 20: 1517-1524
    • (1997) Plant Cell Environ , vol.20 , pp. 1517-1524
    • Coupe, S.A.1    Taylor, J.E.2    Roberts, J.A.3
  • 12
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugar and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugar and related substances. Anal Chem 28: 350-356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 13
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224: 149-155
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 14
    • 0032507714 scopus 로고    scopus 로고
    • Mutation of either of two essential glutamates converts the catalytic domain of tobacco class I chitinase into a chitin-binding lectin
    • Iseli-Gamboni B, Boller T, Neuhaus J-M (1998) Mutation of either of two essential glutamates converts the catalytic domain of tobacco class I chitinase into a chitin-binding lectin. Plant Sci 134: 1171-1178
    • (1998) Plant Sci , vol.134 , pp. 1171-1178
    • Iseli-Gamboni, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 15
    • 0028446563 scopus 로고
    • Potato lectin: A modular protein sharing sequence similarities with the extensin family, the hevein lectin family, and snake venom disintegrins (platelet aggregation inhibitors)
    • Kieliszewski MJ, Showalter AM, Leykam JF (1994) Potato lectin: a modular protein sharing sequence similarities with the extensin family, the hevein lectin family, and snake venom disintegrins (platelet aggregation inhibitors). Plant J 5: 849-861
    • (1994) Plant J , vol.5 , pp. 849-861
    • Kieliszewski, M.J.1    Showalter, A.M.2    Leykam, J.F.3
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 18
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24: 946-950
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0030220995 scopus 로고    scopus 로고
    • Proteolytic processing of class IV chitinase in the compatible interaction of bean roots with Fusarium solani
    • Lange J, Mohr U, Wiemken A, Boller T, Vögeli-Lange R (1996) Proteolytic processing of class IV chitinase in the compatible interaction of bean roots with Fusarium solani. Plant Physiol 111: 1135-1144
    • (1996) Plant Physiol , vol.111 , pp. 1135-1144
    • Lange, J.1    Mohr, U.2    Wiemken, A.3    Boller, T.4    Vögeli-Lange, R.5
  • 21
    • 0025940134 scopus 로고
    • Co- and posttranslational processing of the hevein preproprotein of latex of the rubber tree (Hevea brasiliensis)
    • Lee HI, Broekaert WF, Raikhel NV (1991) Co- and posttranslational processing of the hevein preproprotein of latex of the rubber tree (Hevea brasiliensis). J Biol Chem 266: 15944-15948
    • (1991) J Biol Chem , vol.266 , pp. 15944-15948
    • Lee, H.I.1    Broekaert, W.F.2    Raikhel, N.V.3
  • 22
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedure to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot L, Henrissat B, Gaboriaud C, Bissery V, Morgat A, Mornon JP (1990) Hydrophobic cluster analysis: procedure to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72: 555-574
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 23
    • 0026668497 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
  • 24
    • 0031486631 scopus 로고    scopus 로고
    • Plant chitinase consensus sequences
    • Levorson J, Chlan CA (1997) Plant chitinase consensus sequences. Plant Mol Biol Rep 15: 122-133
    • (1997) Plant Mol Biol Rep , vol.15 , pp. 122-133
    • Levorson, J.1    Chlan, C.A.2
  • 28
    • 0023070284 scopus 로고
    • Direct sequencing of denatured plasmid DNA
    • Mierendorf RC, Pfeffer D (1987) Direct sequencing of denatured plasmid DNA. Methods Enzymol 152: 556-562
    • (1987) Methods Enzymol , vol.152 , pp. 556-562
    • Mierendorf, R.C.1    Pfeffer, D.2
  • 30
    • 0002586488 scopus 로고
    • An unusual lectin from stinging nettle (Urtica dioica) rhizomes
    • Peumans WJ, De Ley M, Broekaert WF (1984) An unusual lectin from stinging nettle (Urtica dioica) rhizomes. FEBS Lett 177: 99-103
    • (1984) FEBS Lett , vol.177 , pp. 99-103
    • Peumans, W.J.1    De Ley, M.2    Broekaert, W.F.3
  • 31
    • 0032549633 scopus 로고    scopus 로고
    • Elderberry (Sambucus nigra) contains truncated Neu5ac(α-2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins
    • Peumans WJ, Roy S, Barre A, Rougé P, Van Leuven F, Van Damme EJM (1998) Elderberry (Sambucus nigra) contains truncated Neu5Ac(α-2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins. FEBS Lett 425: 35-39
    • (1998) FEBS Lett , vol.425 , pp. 35-39
    • Peumans, W.J.1    Roy, S.2    Barre, A.3    Rougé, P.4    Van Leuven, F.5    Van Damme, E.J.M.6
  • 36
    • 0027158760 scopus 로고
    • A rapid CTAB DNA isolation technique useful for RAPD fingerprinting and other PCR applications
    • Stewart CN, Via LE (1993) A rapid CTAB DNA isolation technique useful for RAPD fingerprinting and other PCR applications. BioTechniques 14: 748-750
    • (1993) Biotechniques , vol.14 , pp. 748-750
    • Stewart, C.N.1    Via, L.E.2
  • 37
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 38
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 39
    • 0030584096 scopus 로고    scopus 로고
    • The NeuAc (α-2,6)-Gal/GalNAc binding lectin from elderberry (Sambucus nigra) bark is a type 2 ribosome inactivating protein with an unusual specificity and structure
    • Van Damme EJM, Barre A, Rougé P, Van Leuven F, Peumans WJ (1996a) The NeuAc (α-2,6)-Gal/GalNAc binding lectin from elderberry (Sambucus nigra) bark is a type 2 ribosome inactivating protein with an unusual specificity and structure. Eur J Biochem 235: 128-137
    • (1996) Eur J Biochem , vol.235 , pp. 128-137
    • Van Damme, E.J.M.1    Barre, A.2    Rougé, P.3    Van Leuven, F.4    Peumans, W.J.5
  • 40
    • 0029883541 scopus 로고    scopus 로고
    • Characterization and molecular cloning of SNAV (nigrin b), a GalNAc-specific type 2 ribosome-inactivating protein from the bark of elderberry (Sambucus nigra)
    • Van Damme EJM, Barre A, Rougé P, Van Leuven F, Peumans WJ (1996b) Characterization and molecular cloning of SNAV (nigrin b), a GalNAc-specific type 2 ribosome-inactivating protein from the bark of elderberry (Sambucus nigra). Eur J Biochem 237: 505-513
    • (1996) Eur J Biochem , vol.237 , pp. 505-513
    • Van Damme, E.J.M.1    Barre, A.2    Rougé, P.3    Van Leuven, F.4    Peumans, W.J.5
  • 41
    • 0030964775 scopus 로고    scopus 로고
    • Isolation and molecular cloning of a novel type 2 ribosome-inactivating protein with an inactive B chain from elderberry (Sambucus nigra) bark
    • Van Damme EJM, Barre A, Rougé P, Van Leuven F, Peumans WJ (1997a) Isolation and molecular cloning of a novel type 2 ribosome-inactivating protein with an inactive B chain from elderberry (Sambucus nigra) bark. J Biol Chem 272: 8353-8360
    • (1997) J Biol Chem , vol.272 , pp. 8353-8360
    • Van Damme, E.J.M.1    Barre, A.2    Rougé, P.3    Van Leuven, F.4    Peumans, W.J.5
  • 42
    • 0002241558 scopus 로고
    • Cell-free synthesis of lectins
    • H-J Gabius, S Gabius, eds, Springer-Verlag, Berlin
    • Van Damme EJM, Peumans WJ (1993) Cell-free synthesis of lectins. In H-J Gabius, S Gabius, eds, Lectins and Glycobiology. Springer-Verlag, Berlin, pp 458-468
    • (1993) Lectins and Glycobiology , pp. 458-468
    • Van Damme, E.J.M.1    Peumans, W.J.2
  • 43
    • 0032422738 scopus 로고    scopus 로고
    • Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles
    • Van Damme EJM, Peumans WJ, Barre A, Rougé P (1998) Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit Rev Plant Sci 17: 575-692
    • (1998) Crit Rev Plant Sci , vol.17 , pp. 575-692
    • Van Damme, E.J.M.1    Peumans, W.J.2    Barre, A.3    Rougé, P.4
  • 45
    • 0031436399 scopus 로고    scopus 로고
    • The major elderberry (Sambucus nigra) fruit protein is a lectin derived from a truncated type 2 ribosome-inactivating protein
    • Van Damme EJM, Roy S, Barre A, Rougé P, Van Leuven F, Peumans WJ (1997c) The major elderberry (Sambucus nigra) fruit protein is a lectin derived from a truncated type 2 ribosome-inactivating protein. Plant J 12: 1251-1260
    • (1997) Plant J , vol.12 , pp. 1251-1260
    • Van Damme, E.J.M.1    Roy, S.2    Barre, A.3    Rougé, P.4    Van Leuven, F.5    Peumans, W.J.6
  • 46
    • 34249919394 scopus 로고
    • Hevein: An antifungal protein from rubber-tree (Hevea brasiliensis) latex
    • Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ (1991) Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 183: 258-262
    • (1991) Planta , vol.183 , pp. 258-262
    • Van Parijs, J.1    Broekaert, W.F.2    Goldstein, I.J.3    Peumans, W.J.4
  • 47
    • 0028984728 scopus 로고
    • 1H NMR study of the interaction of NN′N″ triacetylchitotriose with Ac-AMP2, a sugar-binding antimicrobial protein isolated from Amaranthus caudatus
    • 1H NMR study of the interaction of NN′N″ triacetylchitotriose with Ac-AMP2, a sugar-binding antimicrobial protein isolated from Amaranthus caudatus. FEBS Lett 370: 245-249
    • (1995) FEBS Lett , vol.370 , pp. 245-249
    • Verheyden, P.1    Pletinckx, J.2    Maes, D.3    Pepermans, H.A.M.4    Wyns, L.5    Willem, R.6    Martins, J.C.7
  • 49
    • 0025604145 scopus 로고
    • Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity
    • Wirth SJ, Wolf GA (1990) Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity. J Microbiol Methods 12: 197-205
    • (1990) J Microbiol Methods , vol.12 , pp. 197-205
    • Wirth, S.J.1    Wolf, G.A.2
  • 50
    • 0021103515 scopus 로고
    • A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation
    • Wolf P (1983) A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation. Anal Biochem 129: 145-155
    • (1983) Anal Biochem , vol.129 , pp. 145-155
    • Wolf, P.1
  • 51
    • 0021755746 scopus 로고
    • Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II
    • Wright CS (1984) Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II. J Mol Biol 178: 91-104
    • (1984) J Mol Biol , vol.178 , pp. 91-104
    • Wright, C.S.1
  • 52
    • 0025194445 scopus 로고
    • 2.2 å resolution structure analysis of two refined N-acetylneuraminyl-lactose wheat germ agglutinin isolectin complexes
    • Wright CS (1990) 2.2 Å resolution structure analysis of two refined N-acetylneuraminyl-lactose wheat germ agglutinin isolectin complexes. J Mol Biol 215: 635-651
    • (1990) J Mol Biol , vol.215 , pp. 635-651
    • Wright, C.S.1
  • 53
    • 0027268507 scopus 로고
    • Crystallographic refinement and structure analysis of the complex of wheat germ agglutinin with a bivalent sialoglycopeptide from glycophorin A
    • Wright CS, Jaeger J (1993) Crystallographic refinement and structure analysis of the complex of wheat germ agglutinin with a bivalent sialoglycopeptide from glycophorin A. J Mol Biol 232: 620-638
    • (1993) J Mol Biol , vol.232 , pp. 620-638
    • Wright, C.S.1    Jaeger, J.2


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