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Volumn 36, Issue 5, 2009, Pages 851-856

Detection of chitinolytic enzymes with different substrate specificity in tissues of intact sundew (Drosera rotundifolia L.) : CChitinases in sundew tissues

Author keywords

Carnivorous plant; Chitinase expression; Chitinolytic activity; In situ hybridization

Indexed keywords

CHITINASE;

EID: 63949084026     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-008-9254-z     Document Type: Article
Times cited : (26)

References (30)
  • 3
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases-regulation and function
    • A Kasprzewska 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
  • 4
    • 1942480195 scopus 로고    scopus 로고
    • Arabidopsis Chitinases Passarinho PaGenomic Survey
    • Rockville, MD, doi: 10.1199/tab.0023, A.Somerville Cr Meyerowitz EM (eds)
    • Passarinho PA, de Vries SC (2002) Arabidopsis chitinases: a Genomic survey. In: Somerville CR, Meyerowitz EM (eds) The Arabidopsis book. American Society of Plant Biologists, Rockville, MD. doi: 10.1199/tab.0023, http://www.aspb.org/publications/arabidopsis/
    • (2002) The Arabidopsis book. American Society of Plant Biologists
    • De Vries S., C.1
  • 5
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • R Cohen-Kupiec I Chet 1998 The molecular biology of chitin digestion Curr Opin Biotechnol 9 270 277
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 6
    • 14844318174 scopus 로고    scopus 로고
    • The insectivorous sundew (Drosera rotundifolia, L.) might be a novel source of PR genes for biotechnology
    • I Matušíková J Libantová J Moravčíková L Mlynárová JP Nap 2004 The insectivorous sundew (Drosera rotundifolia, L.) might be a novel source of PR genes for biotechnology Biologia 59 719 725
    • (2004) Biologia , vol.59 , pp. 719-725
    • Matušíková, I.1    Libantová, J.2    Moravčíková, J.3    Mlynárová, L.4    Nap, J.P.5
  • 7
    • 28244492028 scopus 로고    scopus 로고
    • Tentacules of in vitro-grown round-leaf sundew (Drosera rotundifolia L.) show induction of chitinase activity upon mimicking the presence of prey
    • I Matušíková J Salaj J Moravčí ková L Mlynárová JP Nap J Libantová 2005 Tentacules of in vitro-grown round-leaf sundew (Drosera rotundifolia L.) show induction of chitinase activity upon mimicking the presence of prey Planta 222 1020 1027
    • (2005) Planta , vol.222 , pp. 1020-1027
    • Matušíková, I.1    Salaj, J.2    Moravčí ková, J.3    Mlynárová, L.4    Nap, J.P.5    Libantová, J.6
  • 8
    • 84982358134 scopus 로고
    • A medium for rapid growth and bioassay with tobacco tissue culture
    • T Murashige F Skoog 1962 A medium for rapid growth and bioassay with tobacco tissue culture Physiol Plant 15 437 497
    • (1962) Physiol Plant , vol.15 , pp. 437-497
    • Murashige, T.1    Skoog, F.2
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quanties protein utilizing the principle-dye binding
    • MM Bradford 1976 A rapid and sensitive method for the quantification of microgram quanties protein utilizing the principle-dye binding Anal Biochem 72 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • UK Laemmli 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
  • 12
    • 0031486631 scopus 로고    scopus 로고
    • Plant chitinase consensus sequences
    • J Levorson CA Chlan 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
  • 13
    • 0001695171 scopus 로고
    • Isolation and characterization of the genes encoding basic and acidic chitinanse in Arabidopsis thaliana
    • DA Samac CM Hironaka PE Yallaly DM Shah 1990 Isolation and characterization of the genes encoding basic and acidic chitinanse 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
  • 14
    • 0001413068 scopus 로고
    • Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter
    • DA Samac DM Shah 1991 Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter Plant Cell 3 1063 1072
    • (1991) Plant Cell , vol.3 , pp. 1063-1072
    • Samac, D.A.1    Shah, D.M.2
  • 19
    • 0025794122 scopus 로고
    • Isolation and characterization of a rice gene encoding a basic chitinase
    • Q Zhu CJ Lamb 1991 Isolation and characterization of a rice gene encoding a basic chitinase Mol Gen Genet 226 289 296
    • (1991) Mol Gen Genet , vol.226 , pp. 289-296
    • Zhu, Q.1    Lamb, C.J.2
  • 20
    • 0029133975 scopus 로고
    • Characterization of a class i chitinase gene and of wound-inducible, root and flower-specific chitinase expression in Brassica napus
    • F Hamel G Bellemare 1995 Characterization of a class I chitinase gene and of wound-inducible, root and flower-specific chitinase expression in Brassica napus Biochim Biophys Acta 1263 212 220
    • (1995) Biochim Biophys Acta , vol.1263 , pp. 212-220
    • Hamel, F.1    Bellemare, G.2
  • 21
    • 0348234696 scopus 로고    scopus 로고
    • Immunohistological localization of chitinase and β-1,3-glucanase in rhizomania-diseased and benzothiadiazole treated sugar beet roots
    • L Burketova K Stillerova M Feltlova 2003 Immunohistological localization of chitinase and β-1,3-glucanase in rhizomania-diseased and benzothiadiazole treated sugar beet roots Physiol Mol Plant Pathol 63 47 54
    • (2003) Physiol Mol Plant Pathol , vol.63 , pp. 47-54
    • Burketova, L.1    Stillerova, K.2    Feltlova, M.3
  • 22
    • 0001227910 scopus 로고
    • Involvement of plant chitinase in sexual reproduction of higher plants
    • DWM Leung 1992 Involvement of plant chitinase in sexual reproduction of higher plants Phytochemistry 31 1899 1900
    • (1992) Phytochemistry , vol.31 , pp. 1899-1900
    • Leung, D.W.M.1
  • 23
    • 0030729789 scopus 로고    scopus 로고
    • Possible correlation between increased vigour and chitinase activity expression in tobacco
    • VR Patil JM Widholm 1997 Possible correlation between increased vigour and chitinase activity expression in tobacco J Exp Bot 48 1943 1950
    • (1997) J Exp Bot , vol.48 , pp. 1943-1950
    • Patil, V.R.1    Widholm, J.M.2
  • 24
    • 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
    • T Taira T Ohnuma T Yamagami Y Aso M Ishiguro M Ishihara 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
  • 25
    • 33747871549 scopus 로고    scopus 로고
    • Isolation and characterization of chitinase genes from pitchers of the carnivorous plant Nepenthes khasiana
    • H Eilenberg S Pnini-Cohen S Schuster A Movtchan A Zilberstein 2006 Isolation and characterization of chitinase genes from pitchers of the carnivorous plant Nepenthes khasiana J Exp Bot 57 2775 2784
    • (2006) J Exp Bot , vol.57 , pp. 2775-2784
    • Eilenberg, H.1    Pnini-Cohen, S.2    Schuster, S.3    Movtchan, A.4    Zilberstein, A.5
  • 26
    • 0031839690 scopus 로고    scopus 로고
    • Production of chitinolytic enzymes and endoglucanase in the soybean rhizosphere in the presence of Trichoderma harzianum and Rhizoctonia solani
    • FK dal Soglio BL Bertagnolli JB Sinclair GZ Yu DM Eastburn 1998 Production of chitinolytic enzymes and endoglucanase in the soybean rhizosphere in the presence of Trichoderma harzianum and Rhizoctonia solani Biol Control 12 111 117
    • (1998) Biol Control , vol.12 , pp. 111-117
    • Dal Soglio, F.K.1    Bertagnolli, B.L.2    Sinclair, J.B.3    Yu, G.Z.4    Eastburn, D.M.5
  • 27
    • 5144224894 scopus 로고    scopus 로고
    • Induction of systemic resistance to Erysiphe orontii cast by application on roots of an isolate of Gliocladium roseum Bainier
    • E Lahoz R Contillo F Porrone 2004 Induction of systemic resistance to Erysiphe orontii cast by application on roots of an isolate of Gliocladium roseum Bainier J Phytopathol 152 465 470
    • (2004) J Phytopathol , vol.152 , pp. 465-470
    • Lahoz, E.1    Contillo, R.2    Porrone, F.3
  • 28
    • 21344497174 scopus 로고
    • Plant chitinases and their roles in resistance to fungal diseases
    • ZK Punja YY Zhang 1993 Plant chitinases and their roles in resistance to fungal diseases J Nematol 25 526 540
    • (1993) J Nematol , vol.25 , pp. 526-540
    • Punja, Z.K.1    Zhang, Y.Y.2
  • 29
    • 0242708845 scopus 로고    scopus 로고
    • The development of Alternaria alternata is prevented by chitinases and β-1,3 glucanase from Citrus limon seedlings
    • N Fanta X Ortega LM Pérez 2003 The development of Alternaria alternata is prevented by chitinases and β-1,3 glucanase from Citrus limon seedlings Biol Res 36 411 420
    • (2003) Biol Res , vol.36 , pp. 411-420
    • Fanta, N.1    Ortega, X.2    Pérez, L.M.3
  • 30
    • 0037334919 scopus 로고    scopus 로고
    • Out of the quagmire of plant defense hypotheses
    • N Stamp 2003 Out of the quagmire of plant defense hypotheses Q Rev Biol 78 23 55
    • (2003) Q Rev Biol , vol.78 , pp. 23-55
    • Stamp, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.