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Volumn 35, Issue 5, 2007, Pages 1660-1672

Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses

Author keywords

[No Author keywords available]

Indexed keywords

ACID PROTEIN; ALANINE; BACTERIAL PROTEIN; PROTEIN P2; RIBOSOME PROTEIN; TRICHOSANTHIN;

EID: 34247135324     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm065     Document Type: Article
Times cited : (67)

References (45)
  • 1
    • 15944368960 scopus 로고    scopus 로고
    • Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties
    • Shaw,P.C., Lee,K.M. and Wong,K.B. (2005) Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties. Toxicon, 45, 683-689.
    • (2005) Toxicon , vol.45 , pp. 683-689
    • Shaw, P.C.1    Lee, K.M.2    Wong, K.B.3
  • 2
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo,Y. and Tsurugi,K. (1987) 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.
    • (1987) J. Biol. Chem , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 3
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo,Y., Mitsui,K., Motizuki,M. and Tsurugi,K. (1987) The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J. Biol. Chem., 262, 5908-5912.
    • (1987) J. Biol. Chem , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 4
    • 77957219651 scopus 로고
    • Modification of ribosomal RNA by ribosome-inactivating proteins from plants
    • Stirpe,F., Bailey,S., Miller,S.P. and Bodley,J.W. (1988) Modification of ribosomal RNA by ribosome-inactivating proteins from plants. Nucleic Acids Res., 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
  • 5
    • 0026549787 scopus 로고
    • The mechanism of action of trichosanthin on eukaryotic ribosomes - RNA N-glycosidase activity of the cytotoxin
    • Zhang,J.S. and Liu,W.Y. (1992) The mechanism of action of trichosanthin on eukaryotic ribosomes - RNA N-glycosidase activity of the cytotoxin. Nucleic Acids Res., 20, 1271-1275.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1271-1275
    • Zhang, J.S.1    Liu, W.Y.2
  • 6
    • 0023947126 scopus 로고
    • The 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. and Tsurugi,K. (1988) The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem., 263, 8735-8739.
    • (1988) J. Biol. Chem , vol.263 , pp. 8735-8739
    • Endo, Y.1    Tsurugi, K.2
  • 7
    • 0015801981 scopus 로고    scopus 로고
    • Sperti,S., Montanaro,L., Mattioli,A. and Stirpe,F. (1973) Inhibition by ricin of protein synthesis in vitro: 60 S ribosomal subunit as the target of the toxin. Biochem. J., 136, 813-815.
    • Sperti,S., Montanaro,L., Mattioli,A. and Stirpe,F. (1973) Inhibition by ricin of protein synthesis in vitro: 60 S ribosomal subunit as the target of the toxin. Biochem. J., 136, 813-815.
  • 8
    • 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. and Nygard,O. (1986) The mechanism of the protein-synthesis elongation cycle in eukaryotes. Effect of ricin on the ribosomal interaction with elongation factors. Eur. J. Biochem., 161, 111-117.
    • (1986) Eur. J. Biochem , vol.161 , pp. 111-117
    • Nilsson, L.1    Nygard, O.2
  • 9
    • 0028519285 scopus 로고
    • Crystal structure of trichosanthin-NADPH complex at 1.7 Å resolution reveals active-site architecture
    • Xiong,J.P., Xia,Z.X. and Wang,Y. (1994) Crystal structure of trichosanthin-NADPH complex at 1.7 Å resolution reveals active-site architecture. Nat. Struct. Biol., 1, 695-700.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 695-700
    • Xiong, J.P.1    Xia, Z.X.2    Wang, Y.3
  • 10
    • 0029013242 scopus 로고
    • Ricin A chain can be chemically cross-linked to the mammalian ribosomal proteins L9 and L10e
    • Vater,C.A., Bartle,L.M., Leszyk,J.D., Lambert,J.M. and Goldmacher,V.S. (1995) Ricin A chain can be chemically cross-linked to the mammalian ribosomal proteins L9 and L10e. J. Biol. Chem., 270, 12933-12940.
    • (1995) J. Biol. Chem , vol.270 , pp. 12933-12940
    • Vater, C.A.1    Bartle, L.M.2    Leszyk, J.D.3    Lambert, J.M.4    Goldmacher, V.S.5
  • 11
    • 0033524919 scopus 로고    scopus 로고
    • Pokeweed antiviral protein accesses ribosomes by binding to L3
    • Hudak,K.A., Dinman,J.D. and Tumer,N.E. (1999) Pokeweed antiviral protein accesses ribosomes by binding to L3. J. Biol. Chem., 274, 3859-3864.
    • (1999) J. Biol. Chem , vol.274 , pp. 3859-3864
    • Hudak, K.A.1    Dinman, J.D.2    Tumer, N.E.3
  • 12
    • 0035822657 scopus 로고    scopus 로고
    • Active center cleft residues of pokeweed antiviral protein mediate its high-affinity binding to the ribosomal protein L3
    • Rajamohan,F., Ozer,Z., Mao,C. and Uckun,F.M. (2001) Active center cleft residues of pokeweed antiviral protein mediate its high-affinity binding to the ribosomal protein L3. Biochemistry, 40, 9104-9114.
    • (2001) Biochemistry , vol.40 , pp. 9104-9114
    • Rajamohan, F.1    Ozer, Z.2    Mao, C.3    Uckun, F.M.4
  • 13
    • 0034854299 scopus 로고    scopus 로고
    • Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B
    • Chan,S.H., Hung,F.S., Chan,D.S. and Shaw,P.C. (2001) Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B. Eur. J. Biochem., 268, 2107-2112.
    • (2001) Eur. J. Biochem , vol.268 , pp. 2107-2112
    • Chan, S.H.1    Hung, F.S.2    Chan, D.S.3    Shaw, P.C.4
  • 14
    • 0036246737 scopus 로고    scopus 로고
    • The acidic ribosomal P proteins
    • Tchorzewski,M. (2002) The acidic ribosomal P proteins. Int. J. Biochem. Cell Biol., 34, 911-915.
    • (2002) Int. J. Biochem. Cell Biol , vol.34 , pp. 911-915
    • Tchorzewski, M.1
  • 15
    • 0031021942 scopus 로고    scopus 로고
    • Binding of mammalian ribosomal protein complex P0.P1.P2 and protein L12 to the GTPase-associated domain of 28 S ribosomal RNA and effect on the accessibility to anti-28 S RNA autoantibody
    • Uchiumi,T. and Kominami,R. (1997) Binding of mammalian ribosomal protein complex P0.P1.P2 and protein L12 to the GTPase-associated domain of 28 S ribosomal RNA and effect on the accessibility to anti-28 S RNA autoantibody. J. Biol. Chem., 272, 3302-3308.
    • (1997) J. Biol. Chem , vol.272 , pp. 3302-3308
    • Uchiumi, T.1    Kominami, R.2
  • 16
    • 0026703192 scopus 로고
    • Direct evidence for interaction of the conserved GTPase domain within 28 S RNA with mammalian ribosomal acidic phosphoproteins and L12
    • Uchiumi,T. and Kominami,R. (1992) Direct evidence for interaction of the conserved GTPase domain within 28 S RNA with mammalian ribosomal acidic phosphoproteins and L12. J. Biol. Chem., 267, 19179-19185.
    • (1992) J. Biol. Chem , vol.267 , pp. 19179-19185
    • Uchiumi, T.1    Kominami, R.2
  • 17
    • 0037040229 scopus 로고    scopus 로고
    • Translation elongation by a hybrid ribosome in which proteins at the GTPase center of the Escherichia coli ribosome are replaced with rat counterparts
    • Uchiumi,T., Honma,S., Nomura,T., Dabbs,E.R. and Hachimori,A. (2002) Translation elongation by a hybrid ribosome in which proteins at the GTPase center of the Escherichia coli ribosome are replaced with rat counterparts. J. Biol. Chem., 277, 3857-3862.
    • (2002) J. Biol. Chem , vol.277 , pp. 3857-3862
    • Uchiumi, T.1    Honma, S.2    Nomura, T.3    Dabbs, E.R.4    Hachimori, A.5
  • 18
    • 0033600919 scopus 로고    scopus 로고
    • Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding
    • Uchiumi,T., Hori,K., Nomura,T. and Hachimori,A. (1999) Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding. J. Biol. Chem., 274, 27578-27582.
    • (1999) J. Biol. Chem , vol.274 , pp. 27578-27582
    • Uchiumi, T.1    Hori, K.2    Nomura, T.3    Hachimori, A.4
  • 20
    • 0025096660 scopus 로고
    • Monoclonal antibodies against acidic phosphoproteins P0, P1, and P2 of eukaryotic ribosomes as functional probes
    • Uchiumi,T., Traut,R.R. and Kominami,R. (1990) Monoclonal antibodies against acidic phosphoproteins P0, P1, and P2 of eukaryotic ribosomes as functional probes. J. Biol. Chem., 265, 89-95.
    • (1990) J. Biol. Chem , vol.265 , pp. 89-95
    • Uchiumi, T.1    Traut, R.R.2    Kominami, R.3
  • 21
    • 0026547431 scopus 로고
    • High level synthesis of biologically active recombinant trichosanthin in Escherichia coli
    • Zhu,R.H., Ng,T.B., Yeung,H.W. and Shaw,P.C. (1992) High level synthesis of biologically active recombinant trichosanthin in Escherichia coli. Int. J. Pept. Protein Res., 39, 77-81.
    • (1992) Int. J. Pept. Protein Res , vol.39 , pp. 77-81
    • Zhu, R.H.1    Ng, T.B.2    Yeung, H.W.3    Shaw, P.C.4
  • 22
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux,B. and Walker,J.E. (1996) Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol., 260, 289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 23
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-protein and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind,M. and Mueller,L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-protein and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. B., 101, 201-205.
    • (1993) J. Magn. Reson. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 24
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek,S. and Bax,A. (1992) Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc., 114, 6291-6293.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 25
    • 0024362326 scopus 로고
    • Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin 1 beta
    • Marion,D., Driscoll,P.C., Kay,L.E., Wingfield,P.T., Bax,A., Gronenborn,A.M. and Clore,G.M. (1989) Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin 1 beta. Biochemistry, 28, 6150-6156.
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1    Driscoll, P.C.2    Kay, L.E.3    Wingfield, P.T.4    Bax, A.5    Gronenborn, A.M.6    Clore, G.M.7
  • 27
    • 4644259437 scopus 로고    scopus 로고
    • Using NMR View to visualize and analyze the NMR spectra of macromolecules
    • Johnson,B.A. (2004) Using NMR View to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol., 278, 313-352.
    • (2004) Methods Mol. Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 28
    • 0010285919 scopus 로고
    • Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR-spectroscopy
    • Bax,A. and Subramanian,S. (1986) Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR-spectroscopy. J. Magn. Reson., 67, 565-569.
    • (1986) J. Magn. Reson , vol.67 , pp. 565-569
    • Bax, A.1    Subramanian, S.2
  • 29
    • 0021754853 scopus 로고
    • Long-range hydrogen-bond mediated effects in peptides - N-15 NMR-study of gramicidin-S in water and organic-solvents
    • Live,D.H., Davis,D.G., Agosta,W.C. and Cowburn,D. (1984) Long-range hydrogen-bond mediated effects in peptides - N-15 NMR-study of gramicidin-S in water and organic-solvents. J. Am. Chem. Soc., 106, 1939-1941.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 1939-1941
    • Live, D.H.1    Davis, D.G.2    Agosta, W.C.3    Cowburn, D.4
  • 30
    • 0002477677 scopus 로고
    • Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles
    • Spedding,G, ed, Oxford University Press, pp
    • Spedding,G. (1990). Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles. In Spedding,G. (ed), Ribosomes and Protein Synthesis Oxford University Press, pp. 9-12.
    • (1990) Ribosomes and Protein Synthesis , pp. 9-12
    • Spedding, G.1
  • 31
    • 0028330374 scopus 로고
    • Structure/function relationship study of Gln156, Glu160 and Glu189 in the active site of trichosanthin
    • Wong,K.B., Ke,Y.B., Dong,Y.C., Li,X.B., Guo,Y.W., Yeung,H.W. and Shaw,P.C. (1994) Structure/function relationship study of Gln156, Glu160 and Glu189 in the active site of trichosanthin. Eur. J. Biochem., 221, 787-791.
    • (1994) Eur. J. Biochem , vol.221 , pp. 787-791
    • Wong, K.B.1    Ke, Y.B.2    Dong, Y.C.3    Li, X.B.4    Guo, Y.W.5    Yeung, H.W.6    Shaw, P.C.7
  • 32
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban,N., Nissen,P., Hansen,J., Moore,P.B. and Steitz,T.A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science, 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 33
    • 0034603171 scopus 로고    scopus 로고
    • Modeling and alanine scanning mutagenesis studies of recombinant pokeweed antiviral protein
    • Rajamohan,F., Pugmire,M.J., Kurinov,I.V. and Uckun,F.M. (2000) Modeling and alanine scanning mutagenesis studies of recombinant pokeweed antiviral protein. J. Biol. Chem., 275, 3382-3390.
    • (2000) J. Biol. Chem , vol.275 , pp. 3382-3390
    • Rajamohan, F.1    Pugmire, M.J.2    Kurinov, I.V.3    Uckun, F.M.4
  • 34
    • 0035968204 scopus 로고    scopus 로고
    • Binding interactions between the active center cleft of recombinant pokeweed antiviral protein and the alpha-sarcin/ricin stem loop of ribosomal RNA
    • Rajamohan,F., Mao,C. and Uckun,F.M. (2001) Binding interactions between the active center cleft of recombinant pokeweed antiviral protein and the alpha-sarcin/ricin stem loop of ribosomal RNA. J. Biol. Chem., 276, 24075-24081.
    • (2001) J. Biol. Chem , vol.276 , pp. 24075-24081
    • Rajamohan, F.1    Mao, C.2    Uckun, F.M.3
  • 36
    • 0022369647 scopus 로고
    • Evidence for the exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver
    • Tsurugi,K. and Ogata,K. (1985) Evidence for the exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver. J. Biochem. (Tokyo), 98, 1427-1431.
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 1427-1431
    • Tsurugi, K.1    Ogata, K.2
  • 37
    • 0034737565 scopus 로고    scopus 로고
    • The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome
    • Savino,C., Federici,L., Ippoliti,R., Lendaro,E. and Tsernoglou,D. (2000) The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome. FEBS Lett., 470, 239-243.
    • (2000) FEBS Lett , vol.470 , pp. 239-243
    • Savino, C.1    Federici, L.2    Ippoliti, R.3    Lendaro, E.4    Tsernoglou, D.5
  • 39
    • 0026469648 scopus 로고
    • X-ray analysis of substrate analogs in the ricin A-chain active site
    • Monzingo,A.F. and Robertus,J.D. (1992) X-ray analysis of substrate analogs in the ricin A-chain active site. J. Mol. Biol., 227 1136-1145.
    • (1992) J. Mol. Biol , vol.227 , pp. 1136-1145
    • Monzingo, A.F.1    Robertus, J.D.2
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson,J.D., Higgins,D.G. and Gibson,T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider,T.D. and Stephens,R.M. (1990) Sequence logos: A new way to display consensus sequences. Nucleic Acids Res., 18, 6097-6100.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 44


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