메뉴 건너뛰기




Volumn 37, Issue 3, 1998, Pages 523-534

A new class II rice chitinase, Rcht2, whose induction by fungal elicitor is abolished by protein phosphatase 1 and 2A inhibitor

Author keywords

Class II chitinase; Defense response; Dephosphorylation; Elicitors; Oryza sativa

Indexed keywords

CHIA4 PROTEIN, ORYZA SATIVA; CHITINASE; COMPLEMENTARY DNA; CYCLOHEXIMIDE; ENZYME INHIBITOR; FUNGAL PROTEIN; MESSENGER RNA; PHOSPHOPROTEIN PHOSPHATASE; VEGETABLE PROTEIN;

EID: 2142773623     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005960313459     Document Type: Review
Times cited : (37)

References (53)
  • 2
    • 7144261583 scopus 로고
    • Purification and characterization of two acidic chitinases having and lacking an N-terminal cysteine-rich domain from root of rice (Oryza saliva L.)
    • Bae CG, Gal SW, Kim CY, Kang CH, Hong JC, Bahk JD, Lee SY, Cho MJ: Purification and characterization of two acidic chitinases having and lacking an N-terminal cysteine-rich domain from root of rice (Oryza saliva L.). Mol Cells 3: 269-274 (1993).
    • (1993) Mol Cells , vol.3 , pp. 269-274
    • Bae, C.G.1    Gal, S.W.2    Kim, C.Y.3    Kang, C.H.4    Hong, J.C.5    Bahk, J.D.6    Lee, S.Y.7    Cho, M.J.8
  • 3
    • 0026251845 scopus 로고
    • The barley lectin carboxyl-terminal propeptide is a vacuolar protein determinant in plants
    • Bednarek SY, Raikhel NV: The barley lectin carboxyl-terminal propeptide is a vacuolar protein determinant in plants. Plant Cell 3: 1195-1206 (1991).
    • (1991) Plant Cell , vol.3 , pp. 1195-1206
    • Bednarek, S.Y.1    Raikhel, N.V.2
  • 4
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitinbinding proteins
    • Beintema JJ: Structural features of plant chitinases and chitinbinding proteins. FEBS Lett 350: 159-163 (1994).
    • (1994) FEBS Lett , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 5
    • 0000358674 scopus 로고
    • Ethylene and the regulation of antifungal hydrolases in plants
    • Boller T: Ethylene and the regulation of antifungal hydrolases in plants. Oxf Surv Plant Mol Cell Biol 5: 145-174 (1988).
    • (1988) Oxf Surv Plant Mol Cell Biol , vol.5 , pp. 145-174
    • Boller, T.1
  • 6
    • 7144262962 scopus 로고    scopus 로고
    • Bryngelsson T, Collinge DB, Green B, Gummesson PO, Kragh K, Thordal-Christensen H: EMBL accession numbers S48847 and S48848 (1994)
    • Bryngelsson T, Collinge DB, Green B, Gummesson PO, Kragh K, Thordal-Christensen H: EMBL accession numbers S48847 and S48848 (1994).
  • 7
    • 0029010727 scopus 로고
    • Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells
    • Chandra S, Low PS: Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells. Proc Natl Acad Sci USA 92: 4120-4123 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4120-4123
    • Chandra, S.1    Low, P.S.2
  • 8
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P: The structure and regulation of protein phosphatases. Annu Rev Biochem 58: 453-508 (1989).
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 10
    • 0030976480 scopus 로고    scopus 로고
    • Protein dephosphorylation mediates salicylic acid-induced expression of PR-1 genes in tobacco
    • Conrath U, Silva H, Klessig DF: Protein dephosphorylation mediates salicylic acid-induced expression of PR-1 genes in tobacco. Plant J 11: 747-757 (1997).
    • (1997) Plant J , vol.11 , pp. 747-757
    • Conrath, U.1    Silva, H.2    Klessig, D.F.3
  • 11
    • 0027665777 scopus 로고
    • Molecular characterization of four chitinase cDNAs obtained from Cladosporium fulvum-infected tomato
    • Danhash N, Wagemakers CAM, van Kan JAC, de Wit PJGM: Molecular characterization of four chitinase cDNAs obtained from Cladosporium fulvum-infected tomato. Plant Mol Biol 22: 1017-1029 (1993).
    • (1993) Plant Mol Biol , vol.22 , pp. 1017-1029
    • Danhash, N.1    Wagemakers, C.A.M.2    Van Kan, J.A.C.3    De Wit, P.J.G.M.4
  • 12
    • 0343916418 scopus 로고
    • Response of protoplasts to hyphal wall components in relationship to resistance of potato to Phytophthora infestans
    • Doke N, Furuichi N: Response of protoplasts to hyphal wall components in relationship to resistance of potato to Phytophthora infestans. Plant Path 21: 23-30 (1982).
    • (1982) Plant Path , vol.21 , pp. 23-30
    • Doke, N.1    Furuichi, N.2
  • 13
    • 0026076198 scopus 로고
    • Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells
    • Felix G, Grosskopf DG, Regenass M, Boller T: Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells. Proc Natl Acad Sci USA 88: 8831-8834 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8831-8834
    • Felix, G.1    Grosskopf, D.G.2    Regenass, M.3    Boller, T.4
  • 14
    • 0025935355 scopus 로고
    • Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells
    • Fukuda Y, Ohme M, Shinshi H: Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells. Plant Mol Biol 16: 1-10 (1991).
    • (1991) Plant Mol Biol , vol.16 , pp. 1-10
    • Fukuda, Y.1    Ohme, M.2    Shinshi, H.3
  • 15
    • 0030431827 scopus 로고    scopus 로고
    • Coordinated activation of chitinase genes and extracellular alkalinization in suspension-cultured tobacco cells
    • Fukuda Y: Coordinated activation of chitinase genes and extracellular alkalinization in suspension-cultured tobacco cells. Biosci Biotech Biochem 60: 2005-2010 (1996).
    • (1996) Biosci Biotech Biochem , vol.60 , pp. 2005-2010
    • Fukuda, Y.1
  • 17
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T, Karin M: The regulation of transcription by phosphorylation. Cell 70: 375-387 (1992).
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 18
    • 0023657398 scopus 로고
    • A cellular DNA-binding protein that activates eukaryotic transcription and DNA replication
    • Jones KA, Kadonaga JT, Rosenfield PJ, Keller JT, Tjian R: A cellular DNA-binding protein that activates eukaryotic transcription and DNA replication. Cell 48: 79-89 (1987).
    • (1987) Cell , vol.48 , pp. 79-89
    • Jones, K.A.1    Kadonaga, J.T.2    Rosenfield, P.J.3    Keller, J.T.4    Tjian, R.5
  • 19
    • 0030065364 scopus 로고    scopus 로고
    • Characterization of two class II chitinase genes from peanut and expression studies in transgenic tobacco plants
    • Kellmann J-W, Kleinow T, Engelhardt K, Philipp C: Characterization of two class II chitinase genes from peanut and expression studies in transgenic tobacco plants. Plant Mol Biol 30: 351-358 (1996).
    • (1996) Plant Mol Biol , vol.30 , pp. 351-358
    • Kellmann, J.-W.1    Kleinow, T.2    Engelhardt, K.3    Philipp, C.4
  • 20
    • 7144228488 scopus 로고    scopus 로고
    • Kombrink E: Direct submission. Accession number U49969 (1996)
    • Kombrink E: Direct submission. Accession number U49969 (1996).
  • 21
    • 0005114584 scopus 로고
    • 2+ uptake and callose synthesis in suspension-cultured cells of Catheranthus roseus are decreased by the protein phosphatase inhibitor okadaic acid
    • 2+ uptake and callose synthesis in suspension-cultured cells of Catheranthus roseus are decreased by the protein phosphatase inhibitor okadaic acid. Plant Physiol 81: 309-312 (1991).
    • (1991) Plant Physiol , vol.81 , pp. 309-312
    • Krauss, H.1    Jeblick, W.2
  • 22
    • 0024979297 scopus 로고
    • Signals and transduction mechanisms for activation of plant defences against microbial attack
    • Lamb CJ, Lawton MA, Dron M, Dixon RA: Signals and transduction mechanisms for activation of plant defences against microbial attack. Cell 56: 215-224 (1989).
    • (1989) Cell , vol.56 , pp. 215-224
    • Lamb, C.J.1    Lawton, M.A.2    Dron, M.3    Dixon, R.A.4
  • 23
    • 0027955308 scopus 로고
    • Plant disease resistance genes in signal perception and transduction
    • Lamb CJ: Plant disease resistance genes in signal perception and transduction. Cell 76: 419-422 (1994).
    • (1994) Cell , vol.76 , pp. 419-422
    • Lamb, C.J.1
  • 24
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with antifungal properties
    • Leah R, Tommerup H, Svendsen I, Mundy J: Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J Biol Chem 266: 1564-1573 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 25
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79: 583-593 (1994).
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.A.3    Lamb, C.4
  • 26
    • 0027096275 scopus 로고
    • Cantharidin-binding protein: Identification as a protein phosphatase 2A
    • Li YM, Casida JF: Cantharidin-binding protein: identification as a protein phosphatase 2A. Proc Natl Acad Sci USA 89: 11867-11870 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11867-11870
    • Li, Y.M.1    Casida, J.F.2
  • 28
    • 0024971161 scopus 로고
    • Identification of high levels of type 1 and type 2A protein phosphatases in higher plants
    • MacKintosh C and Cohen P: Identification of high levels of type 1 and type 2A protein phosphatases in higher plants. Biochem J 262: 335-339 (1989).
    • (1989) Biochem J , vol.262 , pp. 335-339
    • MacKintosh, C.1    Cohen, P.2
  • 29
    • 0026059954 scopus 로고
    • Plant protein phosphatase: Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase
    • MacKintosh C, Coggins J, Cohen P: Plant protein phosphatase: Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase. Biochem J 273: 733-738 (1991).
    • (1991) Biochem J , vol.273 , pp. 733-738
    • MacKintosh, C.1    Coggins, J.2    Cohen, P.3
  • 30
    • 0025605012 scopus 로고
    • Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A
    • MacKintosh RW, Haycox G, Hardie DG, Cohen PTW: Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A. FEBS Lett 276: 156-160 (1990).
    • (1990) FEBS Lett , vol.276 , pp. 156-160
    • MacKintosh, R.W.1    Haycox, G.2    Hardie, D.G.3    Cohen, P.T.W.4
  • 31
    • 84957882027 scopus 로고
    • Ethylene: Symptom, not signal for the induction of chitinase and β-1,3-glucanase in pea pods by pathogens and elicitors
    • Mauch F, Hadwiger LA, Boller T: Ethylene: symptom, not signal for the induction of chitinase and β-1,3-glucanase in pea pods by pathogens and elicitors. Plant Physiol 76: 607-611 (1984).
    • (1984) Plant Physiol , vol.76 , pp. 607-611
    • Mauch, F.1    Hadwiger, L.A.2    Boller, T.3
  • 32
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combination of chitinase and β-1,3-glucanase
    • Mauch F, Mauch-Mani B, Boller T: Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combination of chitinase and β-1,3-glucanase. Plant Physiol 88: 936-942 (1988).
    • (1988) Plant Physiol , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 34
    • 0020050314 scopus 로고
    • A catalogue of splice juction sequences
    • Mount SM: A catalogue of splice juction sequences. Nucl Acids Res 10: 459-472 (1982).
    • (1982) Nucl Acids Res , vol.10 , pp. 459-472
    • Mount, S.M.1
  • 35
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray MG, Thompson WF: Rapid isolation of high molecular weight plant DNA. Nucl Acids Res 8: 4321-4325 (1980).
    • (1980) Nucl Acids Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 36
    • 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, Boller T: 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).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10362-10366
    • Neuhaus, J.-M.1    Sticher, L.2    Meins, F.3    Boller, T.4
  • 37
    • 0000117228 scopus 로고
    • Rice chitinase gene: cDNA cloning and stress-induced expression
    • Nishizawa Y, Hibi T: Rice chitinase gene: cDNA cloning and stress-induced expression. Plant Sci 76: 211-218 (1991).
    • (1991) Plant Sci , vol.76 , pp. 211-218
    • Nishizawa, Y.1    Hibi, T.2
  • 38
    • 0027507719 scopus 로고
    • Sequence variation, differential expression and chromosomal location of rice chitinase genes
    • Nishizawa Y, Kishimoto N, Saito A, Hibi T: Sequence variation, differential expression and chromosomal location of rice chitinase genes. Mol Gen Genet 241: 1-10 (1993).
    • (1993) Mol Gen Genet , vol.241 , pp. 1-10
    • Nishizawa, Y.1    Kishimoto, N.2    Saito, A.3    Hibi, T.4
  • 39
    • 0025129241 scopus 로고
    • Isolation of complementary DNA clones encoding pathogenesis-related proteins P and Q, two acidic chitinases from tobacco
    • Payne G, Ahl P, Moyer M, Harper A, Beck J, Meins F, Ryals J: Isolation of complementary DNA clones encoding pathogenesis-related proteins P and Q, two acidic chitinases from tobacco. Proc Natl Acad Sci USA 87: 98-102 (1990).
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 98-102
    • Payne, G.1    Ahl, P.2    Moyer, M.3    Harper, A.4    Beck, J.5    Meins, F.6    Ryals, J.7
  • 40
    • 21344497174 scopus 로고
    • Plant chitinases and their roles in resistance to fungal diseases
    • Punja ZK, Zhang Y-Y: Plant chitinases and their roles in resistance to fungal diseases. J Nematol 25: 526-540 (1993).
    • (1993) J Nematol , vol.25 , pp. 526-540
    • Punja, Z.K.1    Zhang, Y.-Y.2
  • 41
    • 0001806586 scopus 로고
    • Phosphorylation of proteins in plants: Regulatory effects and potential involvement in stimulus/response coupling
    • Ranjeva R and Boudet AM: Phosphorylation of proteins in plants: regulatory effects and potential involvement in stimulus/response coupling. Annu Rev Plant Physiol 38:73-93 (1987).
    • (1987) Annu Rev Plant Physiol , vol.38 , pp. 73-93
    • Ranjeva, R.1    Boudet, A.M.2
  • 42
    • 0000798386 scopus 로고
    • Ethylene signal is tranduced via protein phosphorylation events in plants
    • Raz V and Fluhr R: Ethylene signal is tranduced via protein phosphorylation events in plants. Plant Cell 5: 523-520 (1993).
    • (1993) Plant Cell , vol.5 , pp. 523-1520
    • Raz, V.1    Fluhr, R.2
  • 43
    • 0026954527 scopus 로고
    • Molecular characterization of type 1 serine/threonine phosphatases from Brassica oleracea
    • Rundle SJ and Nasrallah JB: Molecular characterization of type 1 serine/threonine phosphatases from Brassica oleracea. Plant Mol Biol 20: 367-375 (1992).
    • (1992) Plant Mol Biol , vol.20 , pp. 367-375
    • Rundle, S.J.1    Nasrallah, J.B.2
  • 44
    • 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: Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana. Plant Physiol 93: 907-914 (1990).
    • (1990) Plant Physiol , vol.93 , pp. 907-914
    • Samac, D.A.1    Hironaka, C.M.2    Yallaly, P.E.3    Shah, D.M.4
  • 46
    • 0027323054 scopus 로고
    • Protein phosphatase activity is required for light-inducible gene expression in maize
    • Sheen J: Protein phosphatase activity is required for light-inducible gene expression in maize. EMBO J 12: 3497-3505 (1993).
    • (1993) EMBO J , vol.12 , pp. 3497-3505
    • Sheen, J.1
  • 47
    • 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 JM, Ryals J, Meins F: 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).
    • (1990) Plant Mol Biol , vol.14 , pp. 357-368
    • Shinshi, H.1    Neuhaus, J.M.2    Ryals, J.3    Meins, F.4
  • 48
    • 0027350763 scopus 로고
    • Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana
    • Smith RD, Walker JC: Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana. Plant Mol Biol 21: 307-316 (1993).
    • (1993) Plant Mol Biol , vol.21 , pp. 307-316
    • Smith, R.D.1    Walker, J.C.2
  • 50
    • 0029139330 scopus 로고
    • Studies on elicitor-signal transduction leading to differential expression of defense genes in cultured tobacco cells
    • Suzuki K, Fukuda Y, Shinshi H: Studies on elicitor-signal transduction leading to differential expression of defense genes in cultured tobacco cells. Plant Cell Physiol 36: 281-289 (1995).
    • (1995) Plant Cell Physiol , vol.36 , pp. 281-289
    • Suzuki, K.1    Fukuda, Y.2    Shinshi, H.3
  • 51
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel J, Asselen A: Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal Biochem 178: 362-366 (1989).
    • (1989) Anal Biochem , vol.178 , pp. 362-366
    • Trudel, J.1    Asselen, A.2
  • 52
    • 0030087774 scopus 로고    scopus 로고
    • Regulation, expression and function of a new basic chitinase gene in rice (Oryza sativa L.)
    • Xu Y, Zhu Q, Panbangred W, Shirasu K, Lamb C: Regulation, expression and function of a new basic chitinase gene in rice (Oryza sativa L.). Plant Mol Biol 30: 387-401 (1996).
    • (1996) Plant Mol Biol , vol.30 , pp. 387-401
    • Xu, Y.1    Zhu, Q.2    Panbangred, W.3    Shirasu, K.4    Lamb, C.5
  • 53
    • 0025794122 scopus 로고
    • Isolation and characterization of a rice gene encoding a basic chitinase
    • Zhu Q, Lamb CJ: Isolation and characterization of a rice gene encoding a basic chitinase. Mol Gen Genet 226: 289-296 (1991).
    • (1991) Mol Gen Genet , vol.226 , pp. 289-296
    • Zhu, Q.1    Lamb, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.