메뉴 건너뛰기




Volumn 56, Issue 416, 2005, Pages 1675-1684

Molecular characterization and systemic induction of single-chain ribosome-inactivating proteins (RIPs) in sugar beet (Beta vulgaris) leaves

Author keywords

Beetin; Beta vulgaris; Protein synthesis inhibitor; Ribosome inactivating protein; Sugar beet

Indexed keywords

CELLS; CHARACTERIZATION; POLYPEPTIDES; PROTEINS; RNA; SUGARS; SYNTHESIS (CHEMICAL); VIRUSES;

EID: 20044364755     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/eri164     Document Type: Article
Times cited : (59)

References (52)
  • 1
    • 0013685455 scopus 로고
    • Preparation and optimization of a cell-free translation system from Vicia sativa germ lacking ribosome-inactivating protein activity
    • Arias FJ, Rojo MA, Ferreras JM, Iglesias R, Muñoz R, Girbés T. 1992. Preparation and optimization of a cell-free translation system from Vicia sativa germ lacking ribosome-inactivating protein activity. Journal of Experimental Botany 43, 729-737.
    • (1992) Journal of Experimental Botany , vol.43 , pp. 729-737
    • Arias, F.J.1    Rojo, M.A.2    Ferreras, J.M.3    Iglesias, R.4    Muñoz, R.5    Girbés, T.6
  • 2
    • 0028093888 scopus 로고
    • Isolation and characterization of two new N-glycosidase type 1 ribosome-inactivating proteins unrelated in amino acid sequence from Petrocoptis species
    • Arias FJ, Rojo MA, Ferreras JM, Iglesias R, Muñoz R, Soriano F, Méndez E, Barbieri L, Girbés T. 1994. Isolation and characterization of two new N-glycosidase type 1 ribosome-inactivating proteins unrelated in amino acid sequence from Petrocoptis species. Planta 194, 487-491.
    • (1994) Planta , vol.194 , pp. 487-491
    • Arias, F.J.1    Rojo, M.A.2    Ferreras, J.M.3    Iglesias, R.4    Muñoz, R.5    Soriano, F.6    Méndez, E.7    Barbieri, L.8    Girbés, T.9
  • 3
    • 4243141502 scopus 로고
    • Vicia sativa L. 'run-off' and purified ribosomes: Polyphenylalanine synthesis and molecular action of ribosome-inactivating proteins
    • Arias FJ, Rojo MA, Iglesias R, Ferreras JM, Girbés T. 1993. Vicia sativa L. 'run-off' and purified ribosomes: polyphenylalanine synthesis and molecular action of ribosome-inactivating proteins. Journal of Experimental Botany 44, 1297-1304.
    • (1993) Journal of Experimental Botany , vol.44 , pp. 1297-1304
    • Arias, F.J.1    Rojo, M.A.2    Iglesias, R.3    Ferreras, J.M.4    Girbés, T.5
  • 7
    • 0029809292 scopus 로고    scopus 로고
    • Polynucleotide: Adenosine glycosidase activity of saporin-L1: effect on DNA, RNA and poly(A)
    • Barbieri L, Valbonesi P, Gorini P, Pession A, Stirpe F. 1996. Polynucleotide: adenosine glycosidase activity of saporin-L1: effect on DNA, RNA and poly(A). The Biochemical Journal 319, 507-513.
    • (1996) The Biochemical Journal , vol.319 , pp. 507-513
    • Barbieri, L.1    Valbonesi, P.2    Gorini, P.3    Pession, A.4    Stirpe, F.5
  • 9
    • 85032070757 scopus 로고
    • Effect of pokeweed antiviral protein (PAP) on the infection of plant viruses
    • Chen ZC, Antoniw JF, White RF, Lin Q. 1992. Effect of pokeweed antiviral protein (PAP) on the infection of plant viruses. Plant Pathology 40, 612-620.
    • (1992) Plant Pathology , vol.40 , pp. 612-620
    • Chen, Z.C.1    Antoniw, J.F.2    White, R.F.3    Lin, Q.4
  • 10
    • 0037051943 scopus 로고    scopus 로고
    • The Sambucus nigra type 2 ribosome-inactivating protein SNA-I′ exhibits in planta antiviral activity in transgenic tobacco
    • Chen Y, Peumans W, Van Damme E. 2002. The Sambucus nigra type 2 ribosome-inactivating protein SNA-I′ exhibits in planta antiviral activity in transgenic tobacco. FEBS Letters 516, 27-30.
    • (2002) FEBS Letters , vol.516 , pp. 27-30
    • Chen, Y.1    Peumans, W.2    Van Damme, E.3
  • 11
    • 0032031344 scopus 로고    scopus 로고
    • Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and structurally-related heterodimeric lectin in fruits of Sambucus ebulus L.
    • Citores L, de Benito FM, Iglesias R, Ferreras JM, Argüeso P, Jiménez P, Méndez E, Girbés T. 1998. Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and structurally-related heterodimeric lectin in fruits of Sambucus ebulus L. Planta 204, 310-317.
    • (1998) Planta , vol.204 , pp. 310-317
    • Citores, L.1    De Benito, F.M.2    Iglesias, R.3    Ferreras, J.M.4    Argüeso, P.5    Jiménez, P.6    Méndez, E.7    Girbés, T.8
  • 13
    • 0037044183 scopus 로고    scopus 로고
    • Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin 1
    • Citores L, Ferreras JM, Muñoz R, Benitez J, Jimenez P, Girbés T. 2002. Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin 1. Cancer Letters 184, 29-35.
    • (2002) Cancer Letters , vol.184 , pp. 29-35
    • Citores, L.1    Ferreras, J.M.2    Muñoz, R.3    Benitez, J.4    Jimenez, P.5    Girbés, T.6
  • 14
    • 0028028643 scopus 로고
    • Elderberry (Sambucus nigra L.) seed proteins inhibit protein synthesis and display strong immunoreactivity with rabbit polyclonal antibodies raised against the type 2 ribosome-inactivating protein nigrin b
    • Citores L, Iglesias R, Muñoz R, Ferreras JM, Jiménez P, Girbés T. 1994. Elderberry (Sambucus nigra L.) seed proteins inhibit protein synthesis and display strong immunoreactivity with rabbit polyclonal antibodies raised against the type 2 ribosome-inactivating protein nigrin b. Journal of Experimental Botany 45, 513-516.
    • (1994) Journal of Experimental Botany , vol.45 , pp. 513-516
    • Citores, L.1    Iglesias, R.2    Muñoz, R.3    Ferreras, J.M.4    Jiménez, P.5    Girbés, T.6
  • 15
    • 0026795823 scopus 로고
    • Signal molecules in systemic plant resistance to pathogens and pests
    • Enyedi AJ, Yalpani N, Silverman P, Raskin I. 1992a. Signal molecules in systemic plant resistance to pathogens and pests. Cell 70, 879-886.
    • (1992) Cell , vol.70 , pp. 879-886
    • Enyedi, A.J.1    Yalpani, N.2    Silverman, P.3    Raskin, I.4
  • 16
    • 0026607121 scopus 로고
    • Localization, conjugation and function of salicylic acid in tobacco during hypersensitive reaction to tobacco mosaic virus
    • Enyedi AJ, Yalpani N, Silverman P, Raskin I. 1992b. Localization, conjugation and function of salicylic acid in tobacco during hypersensitive reaction to tobacco mosaic virus. Proceedings of the National Academy of Sciences, USA 89, 2480-2484.
    • (1992) Proceedings of the National Academy of Sciences, USA , vol.89 , pp. 2480-2484
    • Enyedi, A.J.1    Yalpani, N.2    Silverman, P.3    Raskin, I.4
  • 20
    • 2142656302 scopus 로고    scopus 로고
    • Non-toxic type 2 ribosome-inactivating proteins (RIPs) from Sambucus: Occurrence, cellular and molecular activities and uses
    • Girbés T, Ferreras JM, Arias FJ, et al. 2003. Non-toxic type 2 ribosome-inactivating proteins (RIPs) from Sambucus: occurrence, cellular and molecular activities and uses. Cellular and Molecular Biology 49, 537-545.
    • (2003) Cellular and Molecular Biology , vol.49 , pp. 537-545
    • Girbés, T.1    Ferreras, J.M.2    Arias, F.J.3
  • 23
    • 0025311285 scopus 로고
    • Expression and secretion of Mirabilis antiviral protein in Escherichia coli and its inhibition of in vitro eukaryotic and prokaryotic protein synthesis
    • Habuka N, Akiyama K, Tsuge H, Miyano M, Matsumoto T, Noma M. 1990. Expression and secretion of Mirabilis antiviral protein in Escherichia coli and its inhibition of in vitro eukaryotic and prokaryotic protein synthesis. Journal of Biological Chemistry 265, 10988-10992.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 10988-10992
    • Habuka, N.1    Akiyama, K.2    Tsuge, H.3    Miyano, M.4    Matsumoto, T.5    Noma, M.6
  • 25
    • 4344610200 scopus 로고    scopus 로고
    • Cytotoxic ribosome-inactivating lectins from plants
    • Hartley MR, Lord JM. 2004a. Cytotoxic ribosome-inactivating lectins from plants. Biochimica et Biophysica Acta 1701, 1-14.
    • (2004) Biochimica et Biophysica Acta , vol.1701 , pp. 1-14
    • Hartley, M.R.1    Lord, J.M.2
  • 27
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp F, Karas M, Beavis RC, Chait BT. 1991. Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Analytical Chemistry 63, 1193A-1203A.
    • (1991) Analytical Chemistry , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 28
    • 0029665241 scopus 로고    scopus 로고
    • Resistance to geminivirus infection by virus-induced expression of dianthin in transgenic plants
    • Hong Y, Saunders K, Hartley MR, Stanley J. 1996. Resistance to geminivirus infection by virus-induced expression of dianthin in transgenic plants. Virology 220, 119-127.
    • (1996) Virology , vol.220 , pp. 119-127
    • Hong, Y.1    Saunders, K.2    Hartley, M.R.3    Stanley, J.4
  • 29
    • 0029966423 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding a new ribosome-inactivating protein from Beta vulgaris vulgaris (mangold)
    • Hornung E, Wajant H, Jeske H, Mundry KW. 1996. Cloning of a cDNA encoding a new ribosome-inactivating protein from Beta vulgaris vulgaris (mangold). Gene 170, 233-236.
    • (1996) Gene , vol.170 , pp. 233-236
    • Hornung, E.1    Wajant, H.2    Jeske, H.3    Mundry, K.W.4
  • 32
    • 0031104637 scopus 로고    scopus 로고
    • Cloning and characterization of a gene encoding an antiviral protein from Clerodendrum aculeatum L.
    • Kumar D, Verma HN, Tuteja N, Tewari KK. 1997. Cloning and characterization of a gene encoding an antiviral protein from Clerodendrum aculeatum L. Plant Molecular Biology 33, 745-751.
    • (1997) Plant Molecular Biology , vol.33 , pp. 745-751
    • Kumar, D.1    Verma, H.N.2    Tuteja, N.3    Tewari, K.K.4
  • 37
    • 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, 201-208.
    • (1994) The FASEB Journal , vol.8 , pp. 201-208
    • Lord, J.M.1    Roberts, L.M.2    Robertus, J.D.3
  • 39
    • 0030569342 scopus 로고    scopus 로고
    • A systemic antiviral resistance-inducing protein isolated from Clerodendrum inerme Gaertn. is a polynucleotide:adenosine glycosidase (ribosome-inactivating protein)
    • Olivieri F, Prasad V, Valbonesi P, Srivastava S, Ghosal-Chowdhury P, Barbieri L, Bolognesi A, Stirpe F. 1996. A systemic antiviral resistance-inducing protein isolated from Clerodendrum inerme Gaertn. is a polynucleotide:adenosine glycosidase (ribosome-inactivating protein). FEBS Letters 396, 132-134.
    • (1996) FEBS Letters , vol.396 , pp. 132-134
    • Olivieri, F.1    Prasad, V.2    Valbonesi, P.3    Srivastava, S.4    Ghosal-Chowdhury, P.5    Barbieri, L.6    Bolognesi, A.7    Stirpe, F.8
  • 40
    • 0036886340 scopus 로고    scopus 로고
    • Enzymatic specificity of three ribosome-inactivating proteins against fungal ribosomes, and correlation with antifungal activity
    • Park SW, Stevens NM, Vivanco JM. 2002. Enzymatic specificity of three ribosome-inactivating proteins against fungal ribosomes, and correlation with antifungal activity. Planta 216, 227-234.
    • (2002) Planta , vol.216 , pp. 227-234
    • Park, S.W.1    Stevens, N.M.2    Vivanco, J.M.3
  • 41
    • 0028277596 scopus 로고
    • Isolation and characterization of a cDNA clone encoding the pokeweed antiviral protein II from Phytolacca americana and its expression in E. coli
    • Poyet JL, Radom J, Hoeveler A. 1994. Isolation and characterization of a cDNA clone encoding the pokeweed antiviral protein II from Phytolacca americana and its expression in E. coli. FEBS Letters 347, 268-272.
    • (1994) FEBS Letters , vol.347 , pp. 268-272
    • Poyet, J.L.1    Radom, J.2    Hoeveler, A.3
  • 44
    • 0026030363 scopus 로고
    • Cloning of trichosanthin cDNA and its expression in Escherichia coli
    • Shaw PC, Yung MH, Zhu RH, Ho WK, Ng TB, Yeung HW. 1991. Cloning of trichosanthin cDNA and its expression in Escherichia coli. Gene 97, 267-272.
    • (1991) Gene , vol.97 , pp. 267-272
    • Shaw, P.C.1    Yung, M.H.2    Zhu, R.H.3    Ho, W.K.4    Ng, T.B.5    Yeung, H.W.6
  • 45
    • 0033810720 scopus 로고    scopus 로고
    • Systemic induction of a Phytolacca insularis antiviral protein gene by mechanical wounding, jasmonic acid, and abscisic acid
    • Song SK, Choi Y, Moon YH, Kim SG, Choi YD, Lee JS. 2000. Systemic induction of a Phytolacca insularis antiviral protein gene by mechanical wounding, jasmonic acid, and abscisic acid. Plant Molecular Biology 43, 439-450.
    • (2000) Plant Molecular Biology , vol.43 , pp. 439-450
    • Song, S.K.1    Choi, Y.2    Moon, Y.H.3    Kim, S.G.4    Choi, Y.D.5    Lee, J.S.6
  • 46
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins
    • Stirpe F. 2004. Ribosome-inactivating proteins. Toxicon 44, 371-383.
    • (2004) Toxicon , vol.44 , pp. 371-383
    • Stirpe, F.1
  • 47
    • 0029987934 scopus 로고    scopus 로고
    • Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves
    • Stirpe F, Barbieri L, Gorini P, Valbonesi P, Bolognesi A, Polito L. 1996. Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves. FEBS Letters 382, 309-312.
    • (1996) FEBS Letters , vol.382 , pp. 309-312
    • Stirpe, F.1    Barbieri, L.2    Gorini, P.3    Valbonesi, P.4    Bolognesi, A.5    Polito, L.6
  • 48
    • 0027742234 scopus 로고
    • Transgenic plants expressing a functional single-chain Fv antibody are specifically protected from virus attack
    • Tavladoraki P, Benvenuto E, Trinca S, De Martinis D, Cattaneo A, Galeffi P. 1993. Transgenic plants expressing a functional single-chain Fv antibody are specifically protected from virus attack. Nature 366, 469-472.
    • (1993) Nature , vol.366 , pp. 469-472
    • Tavladoraki, P.1    Benvenuto, E.2    Trinca, S.3    De Martinis, D.4    Cattaneo, A.5    Galeffi, P.6
  • 49
    • 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 M. 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, 827-835.
    • (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.6
  • 50
    • 0034571304 scopus 로고    scopus 로고
    • Virus resistance mediated by ribosome inactivating proteins
    • Wang P, Tumer NE. 2000. Virus resistance mediated by ribosome inactivating proteins. Advances in Virus Research 55, 325-355.
    • (2000) Advances in Virus Research , vol.55 , pp. 325-355
    • Wang, P.1    Tumer, N.E.2
  • 52
    • 0033675942 scopus 로고    scopus 로고
    • A non-toxic pokeweed antiviral protein mutant inhibits pathogen infection via a novel salicylic acid-independent pathway
    • Zoubenko O, Hudak K, Tumer NE. 2000. A non-toxic pokeweed antiviral protein mutant inhibits pathogen infection via a novel salicylic acid-independent pathway. Plant Molecular Biology 44, 219-229.
    • (2000) Plant Molecular Biology , vol.44 , pp. 219-229
    • Zoubenko, O.1    Hudak, K.2    Tumer, N.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.