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Volumn 11, Issue 6, 2010, Pages 757-767

Homodimerization of pokeweed antiviral protein as a mechanism to limit depurination of pokeweed ribosomes

Author keywords

[No Author keywords available]

Indexed keywords

POKEWEED ANTIVIRUS PROTEIN; RIBOSOME INACTIVATING PROTEIN 1; VEGETABLE PROTEIN;

EID: 77957305725     PISSN: 14646722     EISSN: 13643703     Source Type: Journal    
DOI: 10.1111/j.1364-3703.2010.00640.x     Document Type: Article
Times cited : (7)

References (37)
  • 1
    • 0027968488 scopus 로고
    • X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23 nm resolution. A model structure provides a suitable electrostatic field for substrate binding
    • Ago H, Kataoka J, Tsuge H, Habuka N, Inagaki E, Noma M, Miyano M. X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23 nm resolution. A model structure provides a suitable electrostatic field for substrate binding. Eur. J. Biochem. 1994, 225:369-374.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 369-374
    • Ago, H.1    Kataoka, J.2    Tsuge, H.3    Habuka, N.4    Inagaki, E.5    Noma, M.6    Miyano, M.7
  • 2
    • 33847383363 scopus 로고    scopus 로고
    • The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity
    • Baykal U, Tumer NE. The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity. Plant J. 2007, 49:995-1007.
    • (2007) Plant J. , vol.49 , pp. 995-1007
    • Baykal, U.1    Tumer, N.E.2
  • 3
    • 0028369223 scopus 로고
    • Pokeweed antiviral protein inactivates pokeweed ribosomes; implications for the antiviral mechanism
    • Bonness MS, Ready MP, Irvin JD, Mabry TJ. Pokeweed antiviral protein inactivates pokeweed ribosomes; implications for the antiviral mechanism. Plant J. 1994, 5:173-183.
    • (1994) Plant J. , vol.5 , pp. 173-183
    • Bonness, M.S.1    Ready, M.P.2    Irvin, J.D.3    Mabry, T.J.4
  • 4
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028026098 scopus 로고
    • Cellular and subcellular distribution of saporins, type-1 ribosome-inactivating proteins, in soapwort (Saponaria officinalis L.)
    • Carzaniga R, Sinclair L, Fordham-Skelton AP, Harris N, Croy RDR. Cellular and subcellular distribution of saporins, type-1 ribosome-inactivating proteins, in soapwort (Saponaria officinalis L.). Planta 1994, 194:461-470.
    • (1994) Planta , vol.194 , pp. 461-470
    • Carzaniga, R.1    Sinclair, L.2    Fordham-Skelton, A.P.3    Harris, N.4    Croy, R.D.R.5
  • 6
    • 0029863815 scopus 로고    scopus 로고
    • Substrate specificity of monomeric and dimeric alpha-sarcin
    • Cheung JI, Wang YR, Lin A. Substrate specificity of monomeric and dimeric alpha-sarcin. FEBS Lett. 1996, 386:60-64.
    • (1996) FEBS Lett. , vol.386 , pp. 60-64
    • Cheung, J.I.1    Wang, Y.R.2    Lin, A.3
  • 7
    • 12544250263 scopus 로고    scopus 로고
    • Inducible expression of a Phytolacca heterotepala ribosome-inactivating protein leads to enhanced resistance against major fungal pathogens in tobacco
    • Corrado G, Delli Bovi P, Ciliento R, Gaudio L, Di Maro A, Aceto S, Lorito M, Rao R. Inducible expression of a Phytolacca heterotepala ribosome-inactivating protein leads to enhanced resistance against major fungal pathogens in tobacco. Phytopathology 2005, 95:206-215.
    • (2005) Phytopathology , vol.95 , pp. 206-215
    • Corrado, G.1    Delli Bovi, P.2    Ciliento, R.3    Gaudio, L.4    Di Maro, A.5    Aceto, S.6    Lorito, M.7    Rao, R.8
  • 8
    • 0030833663 scopus 로고    scopus 로고
    • Identification of a biological inactive complex form of pokeweed antiviral protein
    • Desvoyes B, Poyet JL, Schlick JL, Adami P, Jouvenot M, Dulieu P. Identification of a biological inactive complex form of pokeweed antiviral protein. FEBS Lett. 1997, 410:303-308.
    • (1997) FEBS Lett. , vol.410 , pp. 303-308
    • Desvoyes, B.1    Poyet, J.L.2    Schlick, J.L.3    Adami, P.4    Jouvenot, M.5    Dulieu, P.6
  • 9
    • 0020479406 scopus 로고
    • The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28S ribosomal ribonucleic acid
    • Endo Y, Wool IG. The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28S ribosomal ribonucleic acid. J. Biol. Chem. 1982, 257:9054-9060.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9054-9060
    • Endo, Y.1    Wool, I.G.2
  • 10
    • 0024286995 scopus 로고
    • The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-glycosidase activity of the proteins
    • Endo Y, Tsurugi K, Lambert JM. The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-glycosidase activity of the proteins. Biochem. Biophys. Res. Commun. 1988, 150:1032-1036.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 1032-1036
    • Endo, Y.1    Tsurugi, K.2    Lambert, J.M.3
  • 11
    • 0019332418 scopus 로고
    • Inhibition of elongation factor 2-dependent translocation by the pokeweed antiviral protein and ricin
    • Gessner SL, Irvin JD. Inhibition of elongation factor 2-dependent translocation by the pokeweed antiviral protein and ricin. J. Biol. Chem. 1980, 255:3251-3253.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3251-3253
    • Gessner, S.L.1    Irvin, J.D.2
  • 12
    • 0001238325 scopus 로고
    • Structure, function and applications of ricin and related cytotoxic proteins
    • Griesson D. ed.), New York, Chapman & Hall
    • Hartley MR, Lord JM. Structure, function and applications of ricin and related cytotoxic proteins. Biosynthesis and Manipulation of Plant Products 1993, 210-239. Griesson D, ed.), New York, Chapman & Hall
    • (1993) Biosynthesis and Manipulation of Plant Products , pp. 210-239
    • Hartley, M.R.1    Lord, J.M.2
  • 13
    • 0028086816 scopus 로고
    • Extraction and isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves
    • Hon WC, Griffith M, Chong P, Yang D. Extraction and isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves. Plant Physiol. 1994, 104:971-980.
    • (1994) Plant Physiol. , vol.104 , pp. 971-980
    • Hon, W.C.1    Griffith, M.2    Chong, P.3    Yang, D.4
  • 14
    • 0034022958 scopus 로고    scopus 로고
    • A novel mechanism for inhibition of translation by pokeweed antiviral protein: depurination of the capped RNA template
    • Hudak KA, Wang P, Tumer NE. A novel mechanism for inhibition of translation by pokeweed antiviral protein: depurination of the capped RNA template. RNA 2000, 6:369-380.
    • (2000) RNA , vol.6 , pp. 369-380
    • Hudak, K.A.1    Wang, P.2    Tumer, N.E.3
  • 15
    • 4043177111 scopus 로고    scopus 로고
    • Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity
    • Hudak KA, Parikh BA, Di R, Baricevic M, Santana M, Seskar M, Tumer NE. Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity. Nucleic Acids Res. 2004, 32:4244-4256.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4244-4256
    • Hudak, K.A.1    Parikh, B.A.2    Di, R.3    Baricevic, M.4    Santana, M.5    Seskar, M.6    Tumer, N.E.7
  • 16
    • 0029160529 scopus 로고
    • Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: identification of residues important for toxicity
    • Hur Y, Hwang DJ, Zoubenko O, Coetzer C, Uckun FM, Tumer NE. Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: identification of residues important for toxicity. Proc. Natl. Acad. Sci. USA 1995, 92:8448-8452.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8448-8452
    • Hur, Y.1    Hwang, D.J.2    Zoubenko, O.3    Coetzer, C.4    Uckun, F.M.5    Tumer, N.E.6
  • 17
    • 0016764387 scopus 로고
    • Purification and partial characterization of the antiviral protein from Phytolacca americana which inhibits eukaryotic protein synthesis
    • Irvin JD. Purification and partial characterization of the antiviral protein from Phytolacca americana which inhibits eukaryotic protein synthesis. Arch. Biochem. Biophys. 1975, 169:522-528.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 522-528
    • Irvin, J.D.1
  • 18
    • 58749116652 scopus 로고    scopus 로고
    • Depurination within the intergenic region of Brome mosaic virus RNA3 inhibits viral replication in vitro and in vivo
    • Karran RA, Hudak KA. Depurination within the intergenic region of Brome mosaic virus RNA3 inhibits viral replication in vitro and in vivo. Nucleic Acids Res. 2008, 36:7230-7239.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 7230-7239
    • Karran, R.A.1    Hudak, K.A.2
  • 19
    • 0024840821 scopus 로고
    • Defined mutations in a small region of the Brome Mosaic Virus 2α gene cause diverse temperature-sensitive RNA replication phenotypes
    • Kroner P, Richards D, Traynor P, Ahlquist P. Defined mutations in a small region of the Brome Mosaic Virus 2α gene cause diverse temperature-sensitive RNA replication phenotypes. J. Virol. 1989, 63:5302-5309.
    • (1989) J. Virol. , vol.63 , pp. 5302-5309
    • Kroner, P.1    Richards, D.2    Traynor, P.3    Ahlquist, P.4
  • 20
    • 0021925967 scopus 로고
    • Precursors of ricin and Ricinus communis agglutinin. Glycosylation and processing during synthesis and intracellular transport
    • Lord JM. Precursors of ricin and Ricinus communis agglutinin. Glycosylation and processing during synthesis and intracellular transport. Eur. J. Biochem. 1985, 146:411-416.
    • (1985) Eur. J. Biochem. , vol.146 , pp. 411-416
    • Lord, J.M.1
  • 21
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: stability, specificity, and biological implications
    • Mason JM, Arndt KM. Coiled coil domains: stability, specificity, and biological implications. Chembiochem 2004, 5:170-176.
    • (2004) Chembiochem , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 23
    • 0035136011 scopus 로고    scopus 로고
    • Maize ribosome-inactivating protein 1 has antifungal activity against Aspergillus flavus and Aspergillus nidulans
    • Nielsen K, Payne GA, Boston RS. Maize ribosome-inactivating protein 1 has antifungal activity against Aspergillus flavus and Aspergillus nidulans. Mol. Plant-Microbe Interact. 2001, 14:164-172.
    • (2001) Mol. Plant-Microbe Interact. , vol.14 , pp. 164-172
    • Nielsen, K.1    Payne, G.A.2    Boston, R.S.3
  • 24
    • 0022881369 scopus 로고
    • The mechanism of the protein-synthesis elongation cycle in eukaryotes. Effect of ricin on the ribosomal interaction with elongation factors
    • Nilsson L, Nygård O. The mechanism of the protein-synthesis elongation cycle in eukaryotes. Effect of ricin on the ribosomal interaction with elongation factors. Eur. J. Biochem. 1986, 161:111-117.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 111-117
    • Nilsson, L.1    Nygård, O.2
  • 25
    • 0036828767 scopus 로고    scopus 로고
    • Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the alpha-sarcin/ricin loop of rRNA
    • Parikh BA, Coetzer C, Tumer NE. Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the alpha-sarcin/ricin loop of rRNA. J. Biol. Chem. 2002, 277:41 428-41 437.
    • (2002) J. Biol. Chem. , vol.277
    • Parikh, B.A.1    Coetzer, C.2    Tumer, N.E.3
  • 26
    • 21244490435 scopus 로고    scopus 로고
    • Pokeweed antiviral protein inhibits brome mosaic virus replication in plant cells
    • Picard D, Kao CC, Hudak KA. Pokeweed antiviral protein inhibits brome mosaic virus replication in plant cells. J. Biol. Chem. 2005, 280:20 069-20 075.
    • (2005) J. Biol. Chem. , vol.280
    • Picard, D.1    Kao, C.C.2    Hudak, K.A.3
  • 27
    • 0026625378 scopus 로고
    • Type 1 ribosome-inactivating proteins depurinate plant 25S rRNA without species specificity
    • Prestle J, Schonfelder M, Adam G, Mundry K-W. Type 1 ribosome-inactivating proteins depurinate plant 25S rRNA without species specificity. Nucleic Acids Res. 1992, 20:3179-3182.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3179-3182
    • Prestle, J.1    Schonfelder, M.2    Adam, G.3    Mundry, K.-.W.4
  • 28
    • 0020570288 scopus 로고
    • Requirements for antiribosomal activity of pokeweed antiviral protein
    • Ready MP, Bird S, Rothe G, Robertus JD. Requirements for antiribosomal activity of pokeweed antiviral protein. Biochim. Biophys. Acta 1983, 740:19-28.
    • (1983) Biochim. Biophys. Acta , vol.740 , pp. 19-28
    • Ready, M.P.1    Bird, S.2    Rothe, G.3    Robertus, J.D.4
  • 29
    • 0021768617 scopus 로고
    • Dodecandrin, a new ribosome-inactivating protein from Phytolacca dodecandra
    • Ready MP, Adams RP, Robertus JD. Dodecandrin, a new ribosome-inactivating protein from Phytolacca dodecandra. Biochim. Biophys. Acta 1984, 791:314-319.
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 314-319
    • Ready, M.P.1    Adams, R.P.2    Robertus, J.D.3
  • 31
    • 0020586939 scopus 로고
    • The primary structure of the cytotoxin α-sarcin
    • Sacco G, Drickamer K, Wool IG. The primary structure of the cytotoxin α-sarcin. J. Biol. Chem. 1983, 258:5811-5818.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5811-5818
    • Sacco, G.1    Drickamer, K.2    Wool, I.G.3
  • 32
    • 7044270454 scopus 로고    scopus 로고
    • A transient expression assay using Arabidopsis mesophyll protoplasts
    • Available from URL: (accessed on Jun 14, 2010
    • Sheen J. A transient expression assay using Arabidopsis mesophyll protoplasts. 2002, http://genetics.mgh.harvard.edu/sheenweb/, Available from URL: (accessed on Jun 14, 2010
    • (2002)
    • Sheen, J.1
  • 33
    • 77957219651 scopus 로고
    • Modification of ribosomal RNA by ribosome-inactivating proteins from plants
    • Stirpe F, Bailey S, Miller SP, Bodley JW. Modification of ribosomal RNA by ribosome-inactivating proteins from plants. Nucleic Acids Res. 1988, 16:1349-1357.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1349-1357
    • Stirpe, F.1    Bailey, S.2    Miller, S.P.3    Bodley, J.W.4
  • 34
    • 0025187932 scopus 로고
    • Depurination of plant ribosomes by pokeweed antiviral protein
    • Taylor BE, Irvin JD. Depurination of plant ribosomes by pokeweed antiviral protein. FEBS Lett. 1990, 273:144-146.
    • (1990) FEBS Lett. , vol.273 , pp. 144-146
    • Taylor, B.E.1    Irvin, J.D.2
  • 35
    • 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. Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection. Plant J. 1994, 5:827-835.
    • (1994) Plant J. , 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
  • 36
    • 0030994026 scopus 로고    scopus 로고
    • C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes
    • Tumer NE, Hwang D-J, Bonness M. C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes. Proc. Natl. Acad. Sci. USA 1997, 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
  • 37
    • 0030881586 scopus 로고    scopus 로고
    • Plant resistance to fungal infection induced by nontoxic pokeweed antiviral protein mutants
    • Zoubenko O, Uckun F, Hur Y, Chet I, Tumer N. Plant resistance to fungal infection induced by nontoxic pokeweed antiviral protein mutants. Nat. Biotechnol. 1997, 15:992-996.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 992-996
    • Zoubenko, O.1    Uckun, F.2    Hur, Y.3    Chet, I.4    Tumer, N.5


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