메뉴 건너뛰기




Volumn 49, Issue 326, 1998, Pages 1473-1480

The enemy within: Ricin and plant cells

Author keywords

Castor oil plant; Inhibitor; Membrane transport; Ribosome inactivating protein; Ricin; Seeds

Indexed keywords

MAMMALIA; PHASEOLUS (ANGIOSPERM); RICINUS COMMUNIS;

EID: 0031829027     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/49.326.1473     Document Type: Review
Times cited : (23)

References (67)
  • 1
    • 0026815648 scopus 로고
    • A maize ribosome-inactivating protein is controlled by the transcriptional activator opaque-2
    • Bass HW, Webster C, O'Brian GR, Roberts JKM, Boston RS. 1992. A maize ribosome-inactivating protein is controlled by the transcriptional activator opaque-2. The Plant Cell 4, 225-34.
    • (1992) The Plant Cell , vol.4 , pp. 225-234
    • Bass, H.W.1    Webster, C.2    O'Brian, G.R.3    Roberts, J.K.M.4    Boston, R.S.5
  • 2
    • 0019459694 scopus 로고
    • Immunotoxins: Hybrid molecules of monoclonal antibodies and a toxin subunit specifically kill tumour cells
    • Blythman HE, Casellas P, Gros P, Gros O, Jansen FK, Paolucci F, Pam B, Vidal H. 1981. Immunotoxins: hybrid molecules of monoclonal antibodies and a toxin subunit specifically kill tumour cells. Nature 290, 145-6.
    • (1981) Nature , vol.290 , pp. 145-146
    • Blythman, H.E.1    Casellas, P.2    Gros, P.3    Gros, O.4    Jansen, F.K.5    Paolucci, F.6    Pam, B.7    Vidal, H.8
  • 3
    • 0028369223 scopus 로고
    • Pokeweed antiviral protein inactivates pokeweed ribosomes; implications for the antiviral mechanism
    • Bonness MS, Ready MP, Irvin JD, Mabry TJ. 1994. Pokeweed antiviral protein inactivates pokeweed ribosomes; implications for the antiviral mechanism. The Plant Journal 5, 173-83.
    • (1994) The Plant Journal , vol.5 , pp. 173-183
    • Bonness, M.S.1    Ready, M.P.2    Irvin, J.D.3    Mabry, T.J.4
  • 7
    • 0023947126 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain: The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA
    • Endo, Y, Tsurugi T. 1988. RNA N-glycosidase activity of ricin A-chain: the characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. Journal of Biological Chemistry 263, 8735-9.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 8735-8739
    • Endo, Y.1    Tsurugi, T.2
  • 8
    • 0032486270 scopus 로고    scopus 로고
    • Free ricin A-chain, proricin and native toxin have different cellular fates when expressed in tobacco protoplasts
    • Frigerio L, Vitale A, Lord JM, Ceriotti A, Roberts LM. 1998. Free ricin A-chain, proricin and native toxin have different cellular fates when expressed in tobacco protoplasts. Journal of Biological Chemistry 273, 14194-9.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 14194-14199
    • Frigerio, L.1    Vitale, A.2    Lord, J.M.3    Ceriotti, A.4    Roberts, L.M.5
  • 9
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez L, Chrispeels MJ. 1993. Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. The Plant Cell 5, 1113-24.
    • (1993) The Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 11
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
    • Hara-Nishimura I, Inoue K, Nishimura M. 1991. A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Letters 294, 89-93.
    • (1991) FEBS Letters , vol.294 , pp. 89-93
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 13
    • 0030886889 scopus 로고    scopus 로고
    • Accumulating evidence suggests that several AB- Toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
    • Hazes B, Read RJ. 1997. Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells. Biochemistry 36, 11051-4.
    • (1997) Biochemistry , vol.36 , pp. 11051-11054
    • Hazes, B.1    Read, R.J.2
  • 14
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller MM, Finger A, Schweiger M, Wolf DH. 1996. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-8.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 15
    • 0030993676 scopus 로고    scopus 로고
    • An aspartic endopeptidase is involved in the breakdown of storage proteins in protein-storage vacuoles of plants
    • Hiraiwa N, Kondo M, Nishimura M, Hara-Nishimura I. 1997. An aspartic endopeptidase is involved in the breakdown of storage proteins in protein-storage vacuoles of plants. European Journal of Biochemistry 246, 133-41.
    • (1997) European Journal of Biochemistry , vol.246 , pp. 133-141
    • Hiraiwa, N.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 16
    • 0029328434 scopus 로고
    • Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in tobacco
    • Jach G, Görnhardt B, Mundy J, Logemann J, Pinsdorf E, Leah R, Schell J, Maas C. 1995. Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in tobacco. The Plant Journal 8, 97-109.
    • (1995) The Plant Journal , vol.8 , pp. 97-109
    • Jach, G.1    Görnhardt, B.2    Mundy, J.3    Logemann, J.4    Pinsdorf, E.5    Leah, R.6    Schell, J.7    Maas, C.8
  • 17
  • 20
    • 0026063521 scopus 로고
    • Biochemical and molecular characterisation of three barley seed proteins with antifungal properties
    • Leah R, Tommerup H, Svendsen I, Mundy J. 1991. Biochemical and molecular characterisation of three barley seed proteins with antifungal properties. Journal of Biological Chemistry 266, 1564-73.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 21
    • 14744301682 scopus 로고
    • Expression of a barley ribosome-inactivating protein leads to increased fungal protection in transgenic tobacco plants
    • Logemann J, Jach G, Tommerup H, Mundy J, Schell J. 1992. Expression of a barley ribosome-inactivating protein leads to increased fungal protection in transgenic tobacco plants. Bio/ technology 10, 305-8.
    • (1992) Bio/ technology , vol.10 , pp. 305-308
    • Logemann, J.1    Jach, G.2    Tommerup, H.3    Mundy, J.4    Schell, J.5
  • 22
    • 0021925967 scopus 로고
    • Precursors of ricin and Ricinus communis agglutinin. Glycosylation and processing during synthesis and intracellular transport
    • Lord JM. 1985a. Precursors of ricin and Ricinus communis agglutinin. Glycosylation and processing during synthesis and intracellular transport. European Journal of Biochemistry 146, 411-16.
    • (1985) European Journal of Biochemistry , vol.146 , pp. 411-416
    • Lord, J.M.1
  • 23
    • 0022425309 scopus 로고
    • Synthesis and intracellular transport of lectin and storage protein precursors in endosperm from castor bean
    • Lord JM. 1985b. Synthesis and intracellular transport of lectin and storage protein precursors in endosperm from castor bean. European Journal of Biochemistry 146, 403-9.
    • (1985) European Journal of Biochemistry , vol.146 , pp. 403-409
    • Lord, J.M.1
  • 25
    • 0032559646 scopus 로고    scopus 로고
    • Toxin entry: Retrograde transport through the secretory pathway
    • Lord JM, Roberts LM. 1998. Toxin entry: retrograde transport through the secretory pathway. Journal of Cell Biology 140, 733-6.
    • (1998) Journal of Cell Biology , vol.140 , pp. 733-736
    • Lord, J.M.1    Roberts, L.M.2
  • 26
    • 0028098025 scopus 로고
    • Ricin: Structure, mode of action, and some current applications
    • Lord JM, Roberts LM, Robertus JD. 1994. Ricin: structure, mode of action, and some current applications. The FASEB Journal 8, 201-8.
    • (1994) The FASEB Journal , vol.8 , pp. 201-208
    • Lord, J.M.1    Roberts, L.M.2    Robertus, J.D.3
  • 27
    • 0029199332 scopus 로고
    • Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements
    • Massiah AJ, Hartley MR. 1995. Wheat ribosome-inactivating proteins: seed and leaf forms with different specificities and cofactor requirements. Planta 197, 633-40.
    • (1995) Planta , vol.197 , pp. 633-640
    • Massiah, A.J.1    Hartley, M.R.2
  • 29
    • 0026469648 scopus 로고
    • X-ray analysis of substrate analogs in the ricin A-chain active site
    • Monzingo AF, Robertus JD. 1992. X-ray analysis of substrate analogs in the ricin A-chain active site. Journal of Molecular Biology 227, 1136-45.
    • (1992) Journal of Molecular Biology , vol.227 , pp. 1136-1145
    • Monzingo, A.F.1    Robertus, J.D.2
  • 33
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon M, Schekman R, Romisch K. 1997. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. The EMBO Journal 16, 4540-8.
    • (1997) The EMBO Journal , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Romisch, K.3
  • 34
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-5.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 35
    • 0030929658 scopus 로고    scopus 로고
    • Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol
    • Rapak A, Falnes PO, Olsnes S. 1997. Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol. Proceedings of the National Academy of Sciences, USA 94, 3783-8.
    • (1997) Proceedings of the National Academy of Sciences, USA , vol.94 , pp. 3783-3788
    • Rapak, A.1    Falnes, P.O.2    Olsnes, S.3
  • 37
    • 0025986909 scopus 로고
    • Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action
    • Ready MP, Kim Y, Robertus JD. 1992. Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action. Proteins 10, 270-8.
    • (1992) Proteins , vol.10 , pp. 270-278
    • Ready, M.P.1    Kim, Y.2    Robertus, J.D.3
  • 42
    • 9144270286 scopus 로고
    • Protein biosynthetic capacity in the endosperm tissue of ripening castor bean seeds
    • Roberts LM, Lord JM. 1981a. Protein biosynthetic capacity in the endosperm tissue of ripening castor bean seeds. Planta 152, 420-7.
    • (1981) Planta , vol.152 , pp. 420-427
    • Roberts, L.M.1    Lord, J.M.2
  • 44
    • 0025939115 scopus 로고
    • The structure of ricin B-chain at 2.5 Å resolution
    • Rutenber E, Robertus JD. 1991. The structure of ricin B-chain at 2.5 Å resolution. Proteins 10, 260-9.
    • (1991) Proteins , vol.10 , pp. 260-269
    • Rutenber, E.1    Robertus, J.D.2
  • 47
    • 0023154514 scopus 로고
    • Red light-induced formation of ubiquitin-phytochrome conjugates: Identification of possible intermediates of phytochrome degradation
    • Shanklin J, Jabben M, Vierstra RD. 1987. Red light-induced formation of ubiquitin-phytochrome conjugates: identification of possible intermediates of phytochrome degradation. Proceedings of the National Academy of Sciences, USA 84, 359-63.
    • (1987) Proceedings of the National Academy of Sciences, USA , vol.84 , pp. 359-363
    • Shanklin, J.1    Jabben, M.2    Vierstra, R.D.3
  • 49
    • 0029147513 scopus 로고
    • Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex
    • Simpson JC, Dascher C, Roberts LM, Lord JM, Balch WE. 1995. Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex. Journal of Biological Chemistry 270, 20078-83.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 20078-20083
    • Simpson, J.C.1    Dascher, C.2    Roberts, L.M.3    Lord, J.M.4    Balch, W.E.5
  • 50
    • 0031868419 scopus 로고    scopus 로고
    • Expression of mutant dynamin protects cells against diphtheria toxin but not against ricin
    • in press
    • Simpson JC, Smith DC, Roberts LM, Lord JM. 1998. Expression of mutant dynamin protects cells against diphtheria toxin but not against ricin. Experimental Cell Research (in press).
    • (1998) Experimental Cell Research
    • Simpson, J.C.1    Smith, D.C.2    Roberts, L.M.3    Lord, J.M.4
  • 51
    • 0031397735 scopus 로고    scopus 로고
    • Expression of PAP in transgenic plants induces virus resistance on grafted wild-type plants independent of salicylic acid accumulation and pathogenesis-related protein synthesis
    • Smirnov S, Shulaev V, Tumer NE. 1997 Expression of PAP in transgenic plants induces virus resistance on grafted wild-type plants independent of salicylic acid accumulation and pathogenesis-related protein synthesis. Plant Physiology 114, 1113-21.
    • (1997) Plant Physiology , vol.114 , pp. 1113-1121
    • Smirnov, S.1    Shulaev, V.2    Tumer, N.E.3
  • 53
    • 0025187932 scopus 로고
    • Depurination of plant ribosomes by pokeweed antiviral protein
    • Taylor BE, Irvin JD. 1990. Depurination of plant ribosomes by pokeweed antiviral protein. FEBS Letters 273, 144-6.
    • (1990) FEBS Letters , vol.273 , pp. 144-146
    • Taylor, B.E.1    Irvin, J.D.2
  • 54
    • 0028446541 scopus 로고
    • Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection
    • Taylor S, Massiah A, Lomonossoff G, Roberts LM, Lord JM, Hartley MR. 1994. Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection. The Plant Journal 5, 827-35.
    • (1994) The Plant Journal , vol.5 , pp. 827-835
    • Taylor, S.1    Massiah, A.2    Lomonossoff, G.3    Roberts, L.M.4    Lord, J.M.5    Hartley, M.R.6
  • 55
    • 0026813855 scopus 로고
    • The lectin gene family of Ricinus communis: Cloning of a functional ricin gene and three lectin pseudogenes
    • Tregear JW, Roberts LM. 1992. The lectin gene family of Ricinus communis: cloning of a functional ricin gene and three lectin pseudogenes. Plant Molecular Biology 18, 515-25.
    • (1992) Plant Molecular Biology , vol.18 , pp. 515-525
    • Tregear, J.W.1    Roberts, L.M.2
  • 56
    • 0000013992 scopus 로고
    • Protein bodies of castor bean endosperms. Isolation, fractionation and characterization of protein components
    • Tulley RE, Beevers H. 1976. Protein bodies of castor bean endosperms. Isolation, fractionation and characterization of protein components. Plant Physiology 58, 710-16.
    • (1976) Plant Physiology , vol.58 , pp. 710-716
    • Tulley, R.E.1    Beevers, H.2
  • 58
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in plants: Mechanisms and functions
    • Vierstra RD. 1996. Proteolysis in plants: mechanisms and functions. Plant Molecular Biology 32, 275-302.
    • (1996) Plant Molecular Biology , vol.32 , pp. 275-302
    • Vierstra, R.D.1
  • 59
    • 0000746728 scopus 로고
    • Identification of vacuolar sorting information in phytohaemagglutinin, an unprocessed vacuolar protein
    • von Schaewen A, Chrispeels MJ. 1993. Identification of vacuolar sorting information in phytohaemagglutinin, an unprocessed vacuolar protein. Journal of Experimental Botany 44, 339-42.
    • (1993) Journal of Experimental Botany , vol.44 , pp. 339-342
    • Von Schaewen, A.1    Chrispeels, M.J.2
  • 61
    • 0030043099 scopus 로고    scopus 로고
    • Ricin A-chain fused to a chloroplasttargeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes
    • Walker D, Chaddock AM, Chaddock JA, Roberts LM, Lord JM, Robinson C. 1996. Ricin A-chain fused to a chloroplasttargeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes. Journal of Biological Chemistry 271, 4082-5.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 4082-4085
    • Walker, D.1    Chaddock, A.M.2    Chaddock, J.A.3    Roberts, L.M.4    Lord, J.M.5    Robinson, C.6
  • 62
    • 0026349475 scopus 로고
    • Characterisation and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize
    • Walsh TA, Morgan AE, Hey TD. 1991. Characterisation and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Journal of Biological Chemistry 266, 23422-7.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 23422-23427
    • Walsh, T.A.1    Morgan, A.E.2    Hey, T.D.3
  • 63
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz EJHJ, Jones TR, Sun L, Bogyo M, Geuze HJ, Ploegh HL. 1996a. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-79.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 65
    • 0025975785 scopus 로고
    • Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin and Pseudomonas toxin
    • Yoshida T, Chen C, Zhang M, Wu HC. 1991. Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin and Pseudomonas toxin. Experimental Cell Research 192, 389-95.
    • (1991) Experimental Cell Research , vol.192 , pp. 389-395
    • Yoshida, T.1    Chen, C.2    Zhang, M.3    Wu, H.C.4
  • 66
    • 0000013991 scopus 로고
    • Protein bodies from the endosperm of castor bean. Subfractionation, protein components, lectins and changes during germination
    • Youle RJ, Huang AHC. 1976. Protein bodies from the endosperm of castor bean. Subfractionation, protein components, lectins and changes during germination. Plant Physiology 58, 703-9.
    • (1976) Plant Physiology , vol.58 , pp. 703-709
    • Youle, R.J.1    Huang, A.H.C.2
  • 67
    • 0030881586 scopus 로고    scopus 로고
    • Plant resistance to fungal infection induced by non toxic pokeweed antiviral protein mutant
    • Zoubenko O, Uckum F, Hur Y, Chet I, Tumer N. 1997. Plant resistance to fungal infection induced by non toxic pokeweed antiviral protein mutant. Nature Biotechnology 15, 992-7.
    • (1997) Nature Biotechnology , vol.15 , pp. 992-997
    • Zoubenko, O.1    Uckum, F.2    Hur, Y.3    Chet, I.4    Tumer, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.