메뉴 건너뛰기




Volumn 119, Issue 4, 1999, Pages 1447-1456

Characterization of two novel type I ribosome-inactivating proteins from the storage roots of the Andean crop Mirabilis expansa

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; AMMONIUM SULFATE; CATION EXCHANGE PERFUSION CHROMATOGRAPHY; HOMOGENEITY; ISOELECTRIC POINT; PLANT DEVELOPMENT; PRECIPITATION; PROTEIN ANALYSIS; REVERSED PHASE LIQUID CHROMATOGRAPHY; RIBOSOME INACTIVATING PROTEIN; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 0033117322     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.119.4.1447     Document Type: Article
Times cited : (93)

References (54)
  • 1
    • 0003653070 scopus 로고
    • Sequencing of proteins and peptides
    • TS Work, RH Burdon, eds, Elsevier, Amsterdam, 1981
    • Allen G (1981) Sequencing of proteins and peptides. In TS Work, RH Burdon, eds, Laboratory Techniques in Biochemistry. Elsevier, Amsterdam, 1981, pp 299-318
    • (1981) Laboratory Techniques in Biochemistry , pp. 299-318
    • Allen, G.1
  • 2
    • 85038157461 scopus 로고    scopus 로고
    • Instituto Nacional de Investigacion Agraria, Lima
    • Angeles Millones E (1996) Cultivo del Chago. Instituto Nacional de Investigacion Agraria, Lima
    • (1996) Cultivo del Chago
    • Angeles Millones, E.1
  • 4
    • 0002215662 scopus 로고
    • Inhibition of fungal growth by plant chitinases and β-1,3 glucanases: A morphological study
    • Arlorio M, Ludwing A, Boller T, Bonfante P (1992) Inhibition of fungal growth by plant chitinases and β-1,3 glucanases: a morphological study. Protoplasma 171: 34-43
    • (1992) Protoplasma , vol.171 , pp. 34-43
    • Arlorio, M.1    Ludwing, A.2    Boller, T.3    Bonfante, P.4
  • 5
    • 0020123674 scopus 로고
    • Purification and partial characterization of another form of the antiviral protein from the seeds of Phytolacca americana L. (pokeweed)
    • Barbieri L, Aron GM, Irvin JD, Stirpe F (1982) Purification and partial characterization of another form of the antiviral protein from the seeds of Phytolacca americana L. (pokeweed). Biochem J 203: 55-59
    • (1982) Biochem J , vol.203 , pp. 55-59
    • Barbieri, L.1    Aron, G.M.2    Irvin, J.D.3    Stirpe, F.4
  • 6
    • 0002356221 scopus 로고
    • Ribosome-inactivating proteins from plants
    • M Chessin, D DeBorde, A Zipf, eds, CRC Press, Boca Raton, FL
    • Batelli MG, Stirpe F (1995) Ribosome-inactivating proteins from plants. In M Chessin, D DeBorde, A Zipf, eds, Antiviral Proteins in Higher Plants. CRC Press, Boca Raton, FL, pp 39-64
    • (1995) Antiviral Proteins in Higher Plants , pp. 39-64
    • Batelli, M.G.1    Stirpe, F.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0000431179 scopus 로고
    • A chitin-binding lectin from stinging nettle rhizomes with anti-fungal properties
    • Broekaert WF, Van Parijs J, Leyns F, Joos H, Peumans WJ (1989) A chitin-binding lectin from stinging nettle rhizomes with anti-fungal properties. Science 245: 1100-1102
    • (1989) Science , vol.245 , pp. 1100-1102
    • Broekaert, W.F.1    Van Parijs, J.2    Leyns, F.3    Joos, H.4    Peumans, W.J.5
  • 9
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain: Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo Y, Tsurigi K (1988) RNA N-glycosidase activity of ricin A-chain: mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J Biol Chem 262: 8128-8130
    • (1988) J Biol Chem , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurigi, K.2
  • 10
    • 0007605927 scopus 로고    scopus 로고
    • The future of radical biology? Connecting roots, people, and scientists
    • HE Flores, JP Lynch, D Eissenstat, eds, American Society of Plant Physiologists, Rockville, MD
    • Flores HE, Brigham LA, Vivanco JM (1997) The future of radical biology? Connecting roots, people, and scientists. In HE Flores, JP Lynch, D Eissenstat, eds, Radical Biology: Advances and Perspectives on the Function of Plant Roots. American Society of Plant Physiologists, Rockville, MD, pp 320-339
    • (1997) Radical Biology: Advances and Perspectives on the Function of Plant Roots , pp. 320-339
    • Flores, H.E.1    Brigham, L.A.2    Vivanco, J.M.3
  • 11
    • 0001188522 scopus 로고    scopus 로고
    • Biology and biochemistry of underground plant storage organs
    • T Johns, J Romeo, eds, Plenum Press, New York
    • Flores HE, Flores T (1997) Biology and biochemistry of underground plant storage organs. In T Johns, J Romeo, eds, Functionality of Food Phytochemicals. Plenum Press, New York, pp 113-132
    • (1997) Functionality of Food Phytochemicals , pp. 113-132
    • Flores, H.E.1    Flores, T.2
  • 13
    • 0024615182 scopus 로고
    • Selection and characterization of ricin toxin A-chain mutations in Saccharomyces cerevisiae
    • Frankel A, Schlossman D, Welsh P, Hertler A, Withers D, Johnston S (1989) Selection and characterization of ricin toxin A-chain mutations in Saccharomyces cerevisiae. Mol Cell Biol 9: 415-420
    • (1989) Mol Cell Biol , vol.9 , pp. 415-420
    • Frankel, A.1    Schlossman, D.2    Welsh, P.3    Hertler, A.4    Withers, D.5    Johnston, S.6
  • 14
    • 0025937466 scopus 로고
    • Conserved amino acid residues in ribosome-inactivating proteins from plants
    • Funatsu G, Islam MR, Minami Y, Sung-Sil K, Kimura M (1991) Conserved amino acid residues in ribosome-inactivating proteins from plants. Biochimie 73: 1157-1161
    • (1991) Biochimie , vol.73 , pp. 1157-1161
    • Funatsu, G.1    Islam, M.R.2    Minami, Y.3    Sung-Sil, K.4    Kimura, M.5
  • 15
    • 0002403482 scopus 로고
    • Effects of ribosome inactivating proteins on insect development: Differences between Lepidoptera and Coleoptera
    • Gatehouse AMR, Barbieri L, Stirpe F, Croy RRD (1990) Effects of ribosome inactivating proteins on insect development: differences between Lepidoptera and Coleoptera. Entomol Exp Appl 54: 43-51
    • (1990) Entomol Exp Appl , vol.54 , pp. 43-51
    • Gatehouse, A.M.R.1    Barbieri, L.2    Stirpe, F.3    Croy, R.R.D.4
  • 16
    • 0025864523 scopus 로고
    • Two antifungal thaumatin-like proteins from barley grain
    • Hejgaard J, Jacobsen S, Svendsen I (1991) Two antifungal thaumatin-like proteins from barley grain. FEBS Lett 291: 127-131
    • (1991) FEBS Lett , vol.291 , pp. 127-131
    • Hejgaard, J.1    Jacobsen, S.2    Svendsen, I.3
  • 17
    • 0003010869 scopus 로고
    • Antiviral proteins from Phytolacca
    • M Chessin, D DeBorde, A Zipf, eds, CRC Press, Boca Raton, FL
    • Irvin JD (1995) Antiviral proteins from Phytolacca. In M Chessin, D DeBorde, A Zipf, eds, Antiviral Proteins in Higher Plants. CRC Press, Boca Raton, FL, pp 65-94
    • (1995) Antiviral Proteins in Higher Plants , pp. 65-94
    • Irvin, J.D.1
  • 18
    • 0020081823 scopus 로고
    • Anti-reproductive and other medicinal effects of Tropaeolum tuberosum
    • Johns T, Kitts WD, Newsome F, Towers GHN (1982) Anti-reproductive and other medicinal effects of Tropaeolum tuberosum. J Ethnopharmacol 5: 149-161
    • (1982) J Ethnopharmacol , vol.5 , pp. 149-161
    • Johns, T.1    Kitts, W.D.2    Newsome, F.3    Towers, G.H.N.4
  • 19
    • 0027016664 scopus 로고
    • Adenine depurination and inactivation of plant ribosomes by an antiviral protein of Mirabilis jalapa (MAP)
    • Kataoka J, Habuka N, Miyano M, Masuta C, Koiwai A (1992) Adenine depurination and inactivation of plant ribosomes by an antiviral protein of Mirabilis jalapa (MAP). Plant Mol Biol 20: 1111-1119
    • (1992) Plant Mol Biol , vol.20 , pp. 1111-1119
    • Kataoka, J.1    Habuka, N.2    Miyano, M.3    Masuta, C.4    Koiwai, A.5
  • 20
    • 0025775982 scopus 로고
    • DNA sequence of mirabilis antiviral protein (MAP), a ribosome inactivating protein with antiviral property, from Mirabilis jalapa L. And its expression in E
    • Kataoka J, Habuka N, Miyano M, Takanami Y, Koiwai A (1991) DNA sequence of Mirabilis antiviral protein (MAP), a ribosome inactivating protein with antiviral property, from Mirabilis jalapa L. and its expression in E. coli. J Biol Chem 266: 8426-8430
    • (1991) Coli. J Biol Chem , vol.266 , pp. 8426-8430
    • Kataoka, J.1    Habuka, N.2    Miyano, M.3    Takanami, Y.4    Koiwai, A.5
  • 21
    • 0000234469 scopus 로고
    • Several "pathogenesis-related" proteins in potato are 1,3-β-glucanases and chitinases
    • Kombrick E, Schroeder M, Hahlbrock K (1988) Several "pathogenesis-related" proteins in potato are 1,3-β-glucanases and chitinases. Proc Natl Acad Sci USA 85: 782-786
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 782-786
    • Kombrick, E.1    Schroeder, M.2    Hahlbrock, K.3
  • 23
    • 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
  • 24
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with antifungal activity
    • Leah R, Tommerup H, Svendensen I, Mundy J (1991) Biochemical and molecular characterization of three barley seed proteins with antifungal activity. J Biol Chem 266: 1564-1573
    • (1991) J Biol Chem , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendensen, I.3    Mundy, J.4
  • 26
    • 0027208585 scopus 로고
    • Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein
    • Lodge JK, Kaniewski JK, Turner NE (1993) Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein. Proc Natl Acad Sci USA 90: 7089-7093
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7089-7093
    • Lodge, J.K.1    Kaniewski, J.K.2    Turner, N.E.3
  • 28
    • 0023664808 scopus 로고
    • Purification and characterization of trichosanthin: Homology to the ricin A chain and implications as to mechanism of abortifacient activity
    • Maragonore JM, Joseph J, Bailey MC (1985) Purification and characterization of trichosanthin: homology to the ricin A chain and implications as to mechanism of abortifacient activity. J Biol Chem 262: 11628-11633
    • (1985) J Biol Chem , vol.262 , pp. 11628-11633
    • Maragonore, J.M.1    Joseph, J.2    Bailey, M.C.3
  • 29
    • 84942782727 scopus 로고
    • Antifungal hydrolases in pea tissue. I. Purification and characterization of two chitinases and two β-1,3 glucanases differentially regulated during development in response to fungal infection
    • Mauch F, Hadwiger LA, Boller T (1988a) Antifungal hydrolases in pea tissue. I. Purification and characterization of two chitinases and two β-1,3 glucanases differentially regulated during development in response to fungal infection. Plant Physiol 87: 325-333
    • (1988) Plant Physiol , vol.87 , pp. 325-333
    • Mauch, F.1    Hadwiger, L.A.2    Boller, T.3
  • 30
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase
    • Mauch, F, Mauch-Mani B, Boller T (1988b) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol 88: 936-942
    • (1988) Plant Physiol , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 33
    • 0003826428 scopus 로고
    • National Academy Press, Washington, DC
    • National Research Council (1989) Lost Crops of the Incas. National Academy Press, Washington, DC, pp 22-123
    • (1989) Lost Crops of the Incas , pp. 22-123
  • 34
    • 0026720825 scopus 로고
    • Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from cucurbitaceae plants
    • Ng TB, Chan WY, Yeung HW (1992) Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from Cucurbitaceae plants. Gen Pharmacol 23: 575-590
    • (1992) Gen Pharmacol , vol.23 , pp. 575-590
    • Ng, T.B.1    Chan, W.Y.2    Yeung, H.W.3
  • 35
    • 0027332012 scopus 로고
    • Immunological relatedness of ribosome-inactivating proteins from the Cucurbitaceae family
    • Ng TB, Shaw PC, Yeung HW, Ho WKK (1993) Immunological relatedness of ribosome-inactivating proteins from the Cucurbitaceae family. Biochem Mol Biol Int 31: 447-453
    • (1993) Biochem Mol Biol Int , vol.31 , pp. 447-453
    • Ng, T.B.1    Shaw, P.C.2    Yeung, H.W.3    Ho, W.K.K.4
  • 36
    • 0022962481 scopus 로고
    • Analysis of cytoskeletal structure using blot-purified monospecific antibodies
    • Olmsted JB (1986) Analysis of cytoskeletal structure using blot-purified monospecific antibodies. Methods Enzymol 134: 467-472
    • (1986) Methods Enzymol , vol.134 , pp. 467-472
    • Olmsted, J.B.1
  • 37
    • 0031583821 scopus 로고    scopus 로고
    • Bifunctional plant defense enzymes with chitinase and ribosome inactivating activities from Trichosanthes kirilowii cell cultures
    • Remi Shih NR, McDonald KA, Jackman AP, Girbes T, Iglesias R (1997) Bifunctional plant defense enzymes with chitinase and ribosome inactivating activities from Trichosanthes kirilowii cell cultures. Plant Sci 130: 145-150
    • (1997) Plant Sci , vol.130 , pp. 145-150
    • Remi Shih, N.R.1    McDonald, K.A.2    Jackman, A.P.3    Girbes, T.4    Iglesias, R.5
  • 38
    • 0023052559 scopus 로고
    • Isolation and characterization of two antifungal proteins from barley
    • Roberts WK, Selitrennikoff CP (1986) Isolation and characterization of two antifungal proteins from barley. Biochim Biophys Acta 880: 161-170
    • (1986) Biochim Biophys Acta , vol.880 , pp. 161-170
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 39
    • 0030593702 scopus 로고    scopus 로고
    • DNA-nuclease activity of the single chain ribosome inactivating proteins dianthin 30, saporin 6 and gelonin
    • Roncuzzi L, Gasperi-Campani A (1996) DNA-nuclease activity of the single chain ribosome inactivating proteins dianthin 30, saporin 6 and gelonin. FEBS Lett 392: 16-20
    • (1996) FEBS Lett , vol.392 , pp. 16-20
    • Roncuzzi, L.1    Gasperi-Campani, A.2
  • 40
    • 0028534824 scopus 로고
    • Biosynthesis of defense-related proteins in transformed root cultures of Trichosanthes kirilowii Maxim, var japonicum (kitam.)
    • Savary BJ, Flores HE (1994) Biosynthesis of defense-related proteins in transformed root cultures of Trichosanthes kirilowii Maxim, var japonicum (Kitam.). Plant Physiol 106: 1195-1204
    • (1994) Plant Physiol , vol.106 , pp. 1195-1204
    • Savary, B.J.1    Flores, H.E.2
  • 41
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A, Mauch F, Vogeli 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    Vogeli, U.3    Boller, T.4
  • 42
    • 0028997212 scopus 로고
    • Plant storage proteins
    • Shewry PR (1995) Plant storage proteins. Biol Rev 70: 375-426
    • (1995) Biol Rev , vol.70 , pp. 375-426
    • Shewry, P.R.1
  • 43
    • 0003062516 scopus 로고
    • Andean tuber crops: Worldwide potential
    • J Janick, JE Simon, eds Oregon Timber Press, Portland, OR
    • Sperling CR, King SR (1988) Andean tuber crops: worldwide potential. In J Janick, JE Simon, eds, Advances in New Crops: Research, Development, Economics. Oregon Timber Press, Portland, OR, pp 428-435
    • (1988) Advances in New Crops: Research, Development, Economics , pp. 428-435
    • Sperling, C.R.1    King, S.R.2
  • 44
    • 0022489331 scopus 로고
    • Ribosome-inactivating proteins up to date
    • Stirpe F, Barbieri L (1986) Ribosome-inactivating proteins up to date. FEBS Lett 195: 1-8
    • (1986) FEBS Lett , vol.195 , pp. 1-8
    • Stirpe, F.1    Barbieri, L.2
  • 45
    • 14744291476 scopus 로고
    • Ribosome inactivating proteins from plants: Present status and future prospects
    • Stirpe F, Barbieri L, Batelli MG, Soria M, Lappi DA (1992) Ribosome inactivating proteins from plants: present status and future prospects. Bio/Technology 10: 405-412
    • (1992) Bio/Technology , vol.10 , pp. 405-412
    • Stirpe, F.1    Barbieri, L.2    Batelli, M.G.3    Soria, M.4    Lappi, D.A.5
  • 46
    • 0028853169 scopus 로고
    • Inhibition of Diabrotica larval growth by patatin, the lipid hydrolase from potato tubers
    • Strickland JA, Orr GL, Walsh TA (1995) Inhibition of Diabrotica larval growth by patatin, the lipid hydrolase from potato tubers. Plant Physiol 109: 667-674
    • (1995) Plant Physiol , vol.109 , pp. 667-674
    • Strickland, J.A.1    Orr, G.L.2    Walsh, T.A.3
  • 48
    • 0030994026 scopus 로고    scopus 로고
    • C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate ribosomes
    • Tumer NE, Hwang D-J, Bonness M (1997) C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate ribosomes. Proc Natl Acad Sci USA 94: 3866-3871
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3866-3871
    • Tumer, N.E.1    Hwang, D.-J.2    Bonness, M.3
  • 49
    • 0345412994 scopus 로고
    • Prevention of potato plants from viruses and insect vectors
    • Verma HN, Kymar V (1979) Prevention of potato plants from viruses and insect vectors. J Indian Potato Assoc 6: 157-161
    • (1979) J Indian Potato Assoc , vol.6 , pp. 157-161
    • Verma, H.N.1    Kymar, V.2
  • 51
    • 0002615601 scopus 로고
    • Human diseases due to Serratia: Infection and colonization with Serratia
    • A von Graevenitz, SJ Rubin, eds, CRC Press, Boca Raton, FL
    • von Graevenitz A (1980) Human diseases due to Serratia: infection and colonization with Serratia. In A von Graevenitz, SJ Rubin, eds, The Genus Serratia. CRC Press, Boca Raton, FL, pp 167-186
    • (1980) The Genus Serratia , pp. 167-186
    • Von Graevenitz, A.1
  • 52
    • 0027050494 scopus 로고
    • Characterization of Mirabilis jalapa antiviral protein: A ribosome inactivating protein from Mirabilis jalapa L
    • Wong R, Ng TB, Chan SH, Dong TX, Yeung HW (1992) Characterization of Mirabilis jalapa antiviral protein: a ribosome inactivating protein from Mirabilis jalapa L. Biochem Int 28: 585-593
    • (1992) Biochem Int , vol.28 , pp. 585-593
    • Wong, R.1    Ng, T.B.2    Chan, S.H.3    Dong, T.X.4    Yeung, H.W.5
  • 53
    • 0031081795 scopus 로고    scopus 로고
    • Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): A storage protein with trypsin inhibitor activity
    • Yeh K, Chen J, Lin M, Chen Y, Lin C (1997) Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a storage protein with trypsin inhibitor activity. Plant Mol Biol 33: 565-570
    • (1997) Plant Mol Biol , vol.33 , pp. 565-570
    • Yeh, K.1    Chen, J.2    Lin, M.3    Chen, Y.4    Lin, C.5
  • 54
    • 0030881586 scopus 로고    scopus 로고
    • Plant resistance to fungal infection by nontoxic pokeweed antiviral protein mutants
    • Zoubenko O, Uckun F, Hur Y, Chet I, Turner N (1997) Plant resistance to fungal infection by nontoxic pokeweed antiviral protein mutants. Nat Biotechnol 15: 992-996
    • (1997) Nat Biotechnol , vol.15 , pp. 992-996
    • Zoubenko, O.1    Uckun, F.2    Hur, Y.3    Chet, I.4    Turner, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.