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Volumn 18, Issue 5, 2008, Pages 414-423

A new type of plant chitinase containing LysM domains from a fern (Pteris ryukyuensis): Roles of LysM domains in chitin binding and antifungal activity

Author keywords

Antifungal activity; Chitin binding; Family 18 chitinase; LysM; Plant chitinase

Indexed keywords

CHITIN; CHITINASE; CHITINASE 3B; COMPLEMENTARY DNA; GLYCOSIDASE; NUCLEOTIDE; PROLINE; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 42449095470     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwn018     Document Type: Article
Times cited : (67)

References (31)
  • 1
    • 0032076439 scopus 로고    scopus 로고
    • The sex-inducing pheromone and wounding trigger the same set of genes in the multicellular green alga Volvox
    • Amon P, Haas E, Sumper M. 1998. The sex-inducing pheromone and wounding trigger the same set of genes in the multicellular green alga Volvox Plant Cell. 10:781-789.
    • (1998) Plant Cell , vol.10 , pp. 781-789
    • Amon, P.1    Haas, E.2    Sumper, M.3
  • 2
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound Lytic Murein Transglycosylase D (MltD)
    • Bateman A, Bycroft M. 2000. The structure of a LysM domain from E. coli membrane-bound Lytic Murein Transglycosylase D (MltD). J Mol Biol. 299:1113-1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 3
    • 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
  • 8
    • 0033505252 scopus 로고    scopus 로고
    • Molecular and cellular aspects of the arbuscular mycorrhizal symbiosis
    • Harrison MJ. 1999. Molecular and cellular aspects of the arbuscular mycorrhizal symbiosis. Annu Rev Plant Physiol Plant Mol Biol. 50:361-389.
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 361-389
    • Harrison, M.J.1
  • 9
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J. 293:781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 10
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto T, Yagishita K. 1971. A simple activity measurement of lysozyme. Agric Biol Chem. 33:1154-1156.
    • (1971) Agric Biol Chem , vol.33 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 13
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases: Regulation and function
    • Kasprzewska A. 2003. Plant chitinases: Regulation and function. Cell Mol Biol Lett. 8:809-824.
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 15
    • 0001199167 scopus 로고    scopus 로고
    • HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme
    • Koga D, Yoshioka T, Arakane Y. 1998. HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme. Biosci Biotechnol Biochem. 62:1643-1646.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 1643-1646
    • Koga, D.1    Yoshioka, T.2    Arakane, Y.3
  • 16
    • 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
  • 17
    • 0142240337 scopus 로고    scopus 로고
    • LysM domain receptor kinases regulating rhizobial Nod factor induced infection
    • Limpens E, Franken C, Smit P, Willemse J, Bisseling T, Geurts R. 2003. LysM domain receptor kinases regulating rhizobial Nod factor induced infection. Science. 302:630-633.
    • (2003) Science , vol.302 , pp. 630-633
    • Limpens, E.1    Franken, C.2    Smit, P.3    Willemse, J.4    Bisseling, T.5    Geurts, R.6
  • 20
    • 0022584852 scopus 로고
    • Differences in mRNA levels in Anabaena living freely or in symbiotic association with Azolla
    • Nierzwicki-Bauer SA, Haselkorn R. 1986. Differences in mRNA levels in Anabaena living freely or in symbiotic association with Azolla. EMBO J. 5:29-35.
    • (1986) EMBO J , vol.5 , pp. 29-35
    • Nierzwicki-Bauer, S.A.1    Haselkorn, R.2
  • 21
    • 0035252353 scopus 로고    scopus 로고
    • Horsetails and ferns are a monophyletic-group and the closest living, relatives to seed plants
    • Pryer KM, Schneider H, Smith AR, Cranfill R, Wolf PG, Hunt JS, Sipes SD. 2001. Horsetails and ferns are a monophyletic-group and the closest living, relatives to seed plants. Nature. 409:618-22.
    • (2001) Nature , vol.409 , pp. 618-622
    • Pryer, K.M.1    Schneider, H.2    Smith, A.R.3    Cranfill, R.4    Wolf, P.G.5    Hunt, J.S.6    Sipes, S.D.7
  • 24
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A., Mauch F, Vögeli 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    Vögeli, U.3    Boller, T.4
  • 25
    • 28044450149 scopus 로고    scopus 로고
    • A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases
    • Seidl V, Huemer B, Seiboth B, Kubicek CP. 2005. A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J. 272:5923-5939.
    • (2005) FEBS J , vol.272 , pp. 5923-5939
    • Seidl, V.1    Huemer, B.2    Seiboth, B.3    Kubicek, C.P.4
  • 27
    • 0036561178 scopus 로고    scopus 로고
    • Antifungal activity of rye (Secale cereale) seed chitinases: The different binding manner of class I and class II chitinases to the fungal cell walls
    • Taira T, Ohnuma T, Yamagami T, Aso Y, Ishiguro M, Ishihara M. 2002. Antifungal activity of rye (Secale cereale) seed chitinases: The different binding manner of class I and class II chitinases to the fungal cell walls. Biosci Biotechnol Biochem. 66:970-977.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 970-977
    • Taira, T.1    Ohnuma, T.2    Yamagami, T.3    Aso, Y.4    Ishiguro, M.5    Ishihara, M.6
  • 28
    • 15244357854 scopus 로고    scopus 로고
    • Purification, characterization, and antifungal activity of chitinases from pineapple (Ananas comosus) leaf
    • Taira T, Toma N, Ishihara M. 2005. Purification, characterization, and antifungal activity of chitinases from pineapple (Ananas comosus) leaf. Biosci Biotechnol Biochem. 69:189-196.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 189-196
    • Taira, T.1    Toma, N.2    Ishihara, M.3
  • 29
    • 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
  • 30
    • 0030200167 scopus 로고    scopus 로고
    • Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: Role of the chitin-binding domain in its chitinase action
    • Yamagami T, Funatsu G. 1996. Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: Role of the chitin-binding domain in its chitinase action. Biosci Biotechnot Biochem. 60:1081-1086.
    • (1996) Biosci Biotechnot Biochem , vol.60 , pp. 1081-1086
    • Yamagami, T.1    Funatsu, G.2
  • 31
    • 0032087899 scopus 로고    scopus 로고
    • Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus Tulipa
    • Yamagami T, Ishiguro M. 1998. Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus Tulipa. Biosci Biotechnol Biochem. 62:1253-1257.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 1253-1257
    • Yamagami, T.1    Ishiguro, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.