臺灣博碩士論文加值系統

核醣體抑制蛋白質（ribosome-inactivating proteins；RIPs）之特性是能夠使核醣體（ribosome）失去活性，因而抑制蛋白質的生合成，進而造成細胞死亡。其抑制蛋白質生合成之機制乃因其具有高度專一性的氮-醣??(N-glycosidase)活性，可以水解老鼠細胞核醣體上60S次單元體(60S subunit) 28S rRNA第4324位置上腺嘌呤核?酸(adenosine)的醣?鍵(glycosidic bond)，造成延長因子（elongation factor）EF-2與核醣體結合能力降低，抑制延長因子EF-2水解GTP的能力，使得轉譯過程之延長步驟停止，而抑制蛋白質生合成。
本論文以大腸桿菌表現系統表現出核醣體抑制蛋白質蓖麻子毒蛋白（ricin；RIC）、雞母珠毒蛋白（abrin；ABR）與雞母珠凝集素(Abrus precatorius agglutinin；AAG)及其在核醣體目標區內的數個核醣體蛋白質L9、P0、P1及P2，再以pull-down assay的方式對核醣體抑制蛋白質與核醣體蛋白質之作用關係進行研究；結果顯示核醣體蛋白質L9、P0、P1及P2會與核醣體抑制蛋白質蓖麻子毒蛋白、雞母珠毒蛋白與雞母珠凝集素之間有交互作用。其中雞母珠毒蛋白與核醣體蛋白質P0交互作用較強；而蓖麻子毒蛋白除了與核醣體蛋白質P0交互作用較強外，其與核醣體蛋白質P1交互作用之相對強度亦較雞母珠毒蛋白為高；另外雞母珠凝集素則與核醣體蛋白質L9交互作用較強。我們推測這樣的結果可能是由於不同的核醣體抑制蛋白質與核醣體以不同的方位(orientation)結合所導致。再由雞母珠毒蛋白刪除突變株（deletion mutant）之實驗結果，刪除雞母珠毒蛋白之第三功能部位(domain 3)後，只剩下核醣體蛋白質L9與雞母珠毒蛋白有微弱的交互作用，而刪除雞母珠毒蛋白之第一功能部位(domain 1)則仍然具有與核醣體蛋白質L9、P0、P1及P2交互作用之能力，但交互作用最強的對象則轉變為核醣體蛋白質L9。我們再深入探討雞母珠毒蛋白之組成結構後，結果顯示雞母珠毒蛋白之第一功能部位具有與核醣體蛋白質L9交互作用之能力。

Ribosome-inactivating proteins (RIPs) inhibit protein synthesis and kill the cells by inactivating the ribosome. The mechanism by which RIPs kill cells involves their highly specific N-glycosidase, which is able to hydrolyze the glycosidic bond of the adenine 4324 in 28S rRNA of rat 60S ribosomal subunit and reduces the binding affinity of elongation factor 2 (EF-2) to ribosome and arrests the elongation step of translation.
Several ribosomal proteins (RPs), L9, P0, P1, and P2, in the ribosomal target site of RIPs and three RIPs, ricin (RIC), abrin (ABR), and Abrus precatorius agglutinin (AAG) were expressed by an E. coli expression system. The relationship between RIPs and RPs was studied by pull-down assay. The results apparently indicated that RPs were able to interact with RIPs. RIC, ABR, and AAG were preferred to interacting with P1, P0, and L9, respectively. In conclusion, relative affinities of ABR interacting with L9, P0, P1, and P2 are 1.00, 4.46, 0.42, and 0.48, respectively; however, those of RIC interacting with L9, P0, P1, and P2 are 1.00, 4.44, 2.13, and 0.10, respectively. In addition, those of AAG interacting with L9, P0, P1, and P2 are 1.00, 0.03, 0.09, and 0.02.This difference results from the variety of structures of three RIPs and different binding orientation between RIPs and RPs.
The binding regions on the ABR were mapped by deletion methods. Only L9 interacted with ABR-I-II which was the deletion of domain 3 of ABR. ABR-II-III, domain 1 of ABR deleted, still interacted with L9 strongly while P0, P1, and P2 interacted moderately. It suggests that ABR domain 1 contributed to the interaction between ABR and L9.

一、摘 要 ---------------------------------------------------- 1
二、英文摘要 ---------------------------------------------------- 3
三、縮 寫 ---------------------------------------------------- 5
四、緒 論 ---------------------------------------------------- 7
五、實驗材料 ---------------------------------------------------- 20
六、實驗方法 ---------------------------------------------------- 23
七、實驗結果 ---------------------------------------------------- 42
八、討 論 ---------------------------------------------------- 51
九、圖表及圖表說明 ------------------------------------------- 57
十、參考文獻 ---------------------------------------------------- 85

Agapov, I. I., Tonevitsky, G., Shamshiev, A. T., Pohl, E., Pohl, P., Palmer, R. A., and Kirpichnikov, M. P. (1997) The role of structural domains in RIP II toxin model membrane binding. FEBS Lett. 402 : 91-93
Agnes, D. M., Larergne, J. P., Guillot, D., Sontag, B. L., and Reboud, J. P. (1994) Interaction of phosphorylated elongation factor EF-2 with nucleotides and ribosomes. FEBS Lett. 356 : 283-286
Agrawal, R. K., and Frank, J. (1999) Structural studies of the translational apparatus. Curr. Opin. Struct. Biol. 9(2) : 215-221
Altschul, S. F., Thomas, L. M., Alejandro, A. S., Jinghui, Z., Zheng, Z., Webb, M., and David, J. L. (1997) "Gapped BLAST and PSI-BLAST : a new generation of protein database searchprograms". Nucleic Acids Res. 25 : 3389-3402
Auler, H. (1928) Abrin. Periodico aj medicina chirurgia ed Igiene 35 : 310-312
Barbieri, L., Aron, G. M., Irvin, J. D., and Stripe, 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
Barbieri, L., Battelli, M. G., and Stripe, F. (1993) Ribosome inactivating proteins from plants. Biochim. Biophys. Acta 1154 : 237-282
Barbieri, L., and Stripe, F. (1982) Ribosome-inactivating proteins from plants: properties and possible uses. Cancer Surveys 1 : 489-520
Benatti, L., Saccardo, M. B., Dani, M., Bitti, G. P., Sassano, M., Lorenzetti, R., Lappi, D. A., and Soria, M. (1989) Nucleotide sequence of cDNA doking for saporin-6, a type-I ribosome-inactivating protein from Saponaria officinalis. Eur. J. Biochem. 183 : 465-470
Benson, S., Olsnes, S., Pihl, A., Skorue, J., and Abraham, K. A. (1975) On the mechanism of protein-synthesis inhibition by abrin and ricin. Eur. J. Biochem. 59 : 573-580
Benson, S., Olsnes, S., Pihl, A., Skorve, J., and Abraham, A. K. (1975) On the mechanism of protein-synthesis inhibition by abrin and ricin. Inhibition of the GTP-hydrolysis site on the 60-S ribosomal subunit. Eur. J. Biochem. 59(2) : 573-580
Berheimer, A. (1952) Hemagglutinin in caterpillar bloods. Science 115 : 150-152
Bilge, A., Warner, C. V., and Press, O. W. (1995) Translocation of ricin A-chain into proteoliposome reconstituted from Golgi and endoplasmic reticulum. J. Biol. Chem. 270 : 23720-23725
Boyd, W., and Brown, R. (1965) A specific agglutinin in the snail, Octala lactea. Nature 280 : 584-593
Brosius, J., Dull, T. J., and Voler, H. F. (1980) Complete nucleotide sequence of a 23 S ribosomal RNA gene from Escherichia coli. Proc. Natl. Acad. Sci. USA 77 : 201-204
Canasco, L., Fernandez-Puentes, C., and Vazquez, D. (1975) Effects of ricin on the ribosomal sites involved in the interaction of the elongation factors. Eur. J. Biochem. 54 : 499-503
Chan, L. N. L., Li, J. S., and Liu, S. Y. (1985) Differential effects of abrin on normal and tumor cells. J. Cell Physiol. 123 : 132-138
Chaudhary, V. K., Jinno, Y., FitzGearld, D., and Pastan, I. (1990) Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity. Proc. Natl. Acad. Sci. USA 87 : 308-312
Chow, L. P., Chang, K. H., and Lin, J. Y. (1990) Selective cytotoxic effects of immunotoxin-monoclonal anti-AFP-abrin A chain conjugate on several human hepatoma cell lines. Biochem. Intl. 22 : 95-102
Chow, T. P., Feldman, R. A., Lovett, M., and Piatak, M. (1990) Isolation and DNA sequence of a gene encoding a-trichosanthin, a type I ribosome-inactivating protein. J. Biol. Chem. 265 : 8670-8674
Chung, C. T., Niemela, S. L., and Miller, R. H. (1989) One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA. 86(7) : 2172-2175
Coleman, W. H., and Roberts, W. K. (1982) Inhibitors of animal cell-free protein synthesis from grains. Biochim. Biophys. Acta 696 : 239-244
Collier, R. J. (1967) Effect of diphtheria toxin on protein synthesis : inactivation of one of the transfer factors. J. Mol. Biol. 25 : 83-98
Cushing, J. (1953) Individual variation in the hemagglutinin content of Yellowfin tuna and bloods skipjack. J. Immunol. 68 : 543-544
Draper, R. K., and Simon, M. I. (1980) The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence of lysosomal involvement. J. Cell Biol. 87 : 849-854
Dube, P., Wieske, M., Stark, H., Schatz, M., Stahl, J., Zemlin, F., Lutsch, G., and van Heel, M. (1998) The 80S rat liver ribosome at 25 A resolution by electron cryomicroscopy and angular reconstitution. Structure. 6(3) : 389-399
Endo, Y., Gluck, A., and Wool, I. G. (1991) Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. J. Mol. Biol. 221 : 193-207
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
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
Endo, Y., and Wool, I. G. (1982) The site of action of a-sarcin on eukaryotic ribosomes. J. Biol. Chem. 257 : 9054-9060
Fernandez-Puentes, C., and Carrasco, L. (1980) Viral infection permeabilizes mammalian cells to protein toxins. Cell 20 : 766-795
Fernandez-Puentes, C., Benson, S., Olsnes, S., and Pihl, A. (1976) Protective effect of elongation factor 2 on the inactivation of ribosomes by the toxic lectins abrin and ricin. Eur. J. Biochem. 64 : 437-443
Fitzgerald, D., and Pastan, I. (1989) Targeted toxin therapy for the treatment of cancer J. Natl. Cancer Inst. 81 : 1455-1461
Funatsu, G., Taguchi, Y., Kamenosono, M., and Yanaka, M. (1988) The complete amino acid sequence of A-chain of abrin-a, a toxic protein from the seeds of Abrus precatorius. Agric. Biol. Chem. 52 : 1095-1097
Gasperi-Campani, A., Barbieri, L., Battelli, M. G., and Stirpe, F. (1985) On the distribution of ribosome-inactivating proteins among plants. J. Natl. Prod. 48 : 446-454
Gasperi-Campani, A., Barbieri, L., Lorenzoni, E., Montanaro, L., Sperti, S., Bonetti, E., and Stripe, F. (1978) Modeccin, the toxin of Adenia digitata: purification, toxicity and inhibition of protein synthesis in vitro. Biochem. J. 174 : 491-496
Georgiev, O. I., Nikolaev, N., Hadjiolov, A. A., Skryabin, K. G., Zakharyev, V. M., and Bayer, A. A. (1981) The structure of the yeast ribosomal RNA gene: complete sequence of the 25 S rRNA gene from Saccharomyces cerevisiae. Nucleic Acids Res. 9 : 6953-6958
Gluck, A., Endo, Y., and Wool, I. G. (1992) Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. J. Mol. Biol. 226 : 411-424
Gudkov, A. T., Venyaminov, S. Yu, Amons, R., Moller, W., and Itoh, T. (1981) A physical study of acidic ribosomal proteins from Artemia salina, Bacillus subtilis and Micrococcus lysodeikticus. FEBS Lett. 136 : 235-238
Halling, K. C., Halling, A. C., Murray, E. E., Ladin, B. F., Houston, L. L., and Weaver, R. F. (1985) Genomic cloning and characterization of a ricin gene from Ricinus communis. Nucleic Acids Res. 13 : 8019-8033
Hammeratorm, S., and Kabat, E. (1969) Purification and characterization of a blood group A reactive hemagglutinin from the snail, Helix pomatia, and a study of its combining site. Biochemistry 8 : 2696-2705
Hedblom, M. L., Cawley, D. B., Boguslawski, S., and Houston, L. L. (1978) Binding of ricin A chain to rat liver ribosomes: relationship to ribosome inactivation. J. Supramol. Struct. 9 : 253-268
Heus, H. A., and Pardi, A. (1991) Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops. Science 253 : 191-194
Ho, W. K. K., Liu, S. C., Shaw, P. C., Yeung, H. W., Ng, T. B., and Chan, W. Y. (1991) Cloning of the cDNA of a-momorcharin : a ribosome-inactivating protein. Biochim. Biophys. Acta 1088 : 311-314
Hori, N., Murakawa, K., Matoba, R., Fukushima, A., Okubo, K. and Matsubara, K. (1993) A new human ribosomal protein sequence, homologue of rat L9. Nucleic Acids Res. 21 : 4395
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
Hughes, J. N., Lindsay, C. D., and Griffths, G. D. (1996) Morphology of ricin and abrin exposed endothelial cells in consistent with apoptotic cell death. Human Exp. Toxicol. 15 : 443-451
Hung, C. H., Lec, M. C., Lee, T. C., and Lin, J. Y. (1993) Primary structure of three distinct isoabrins determined by cDNA sequencing. J. Mol. Biol. 229 : 263-267
Husain, J., Tickle, I. J., and Wood, S. P. (1994) Crystal structure of momordin, a type I ribosome inactivating protein from the seeds of Momordica charantia FEBS Lett. 342 : 154-158
Hydgin, R., Pricer, W., Ashwell, G., and Stockat, R. (1974) The isolation and properties of a rabbit liver binding protein specific for asilo-glycoproteins. J. Bilol. Chem. 249 : 5536-5543
Ippoliti, R., Lendaro, E., Bellelli, A., and Brunori, M. (1992) A ribosomal protein is specifically recognized by saporin, a plant toxin which inhibits protein synthesis. FEBS Lett. 298 : 145-148
Irvin, J. D. (1975) Purification and partial characterization of the antiviral protein from Phytolacca americana with inhibits eukaryotic protein synthesis. Arch. Biochem. Biophys. 169 : 522-528
Johnson, H. (1964) Human blood group A specific agglutinin of butter clam, Saxidomus gigantens. Science 146 : 548-549
Kawata, A., Yoshida, M., Okazaki, M., Yotoka, S., Barcos, M., and Seon, B. K. (1994) Establishment of new SCID and nude mouse models of human B leukemia/lymphoma and effective therapy of the tumors with immunotoxin and monoclonal antibody: Marked difference between the SCID and nude mouse models in the antitumor efficacy of monoclonal antibody. Cancer Res. 54 : 2688-2694
Kernan, N. A., Byers, V., Scannon, P. J., Mischak, R. P., Brochstein, J., Flomenberg, N., Dupont, B., and O'Reilly, R. J. (1988) Treatment of steroid-resistant acute graft-vs-host disease by in vivo administration of an anti-T-cell ricin A chain immunotoxin. J. Am. Med. Assoc. 259 : 3154-3157
Koren, E., Reichlin, M. W., Koscec, M., Fugate, R. D., and Reichlin, M. (1992) Autoantibodies to the ribosomal P proteins react with a plasma membrane-related target on human cells. J Clin Invest. 89 : 1236-1241
Lambert, J. M., Goldmacher, V. S., Collinson, A. R., Nadler, L. M., and Blattler, W. A. (1991) An immunotoxin prepared with blocked ricin: A natural plant toxin adapted for therapeutic use. Cancer Res. 51 : 6236-6242
Lee-Huang, S., Kun, H. F., Huang, P. L., Li, B. Q., Huang, P., Huang, H. I., and Chen, H. C. (1991) A new class of anti-HIV agents: GAP31, DAPs30 and 32. FEBS Lett. 291 : 139-144
Lendaro, E., Ippoliti, R., Belleli, A., Brunori, M., Evangelista, V., Guidarini, D., and Benedetti, P. A. (1994) Intracellular dynamics of ricin followed by fluorescence microscopy on living cells reveals a rapid accumulation of the dimeric toxin in the Golgi apparatus. FEBS Lett. 344 : 99-104
Lin, J. Y., Hsieh, Y. S., and Chu, S. S. (1989) Chimeric protein: abrin B chain trypsin inhibitor conjugate as a new antitumor agent. Biochem. Intlel. 19 : 313-323
Lin, J. Y., Lei, L. L., and Tung, T. C. (1969) Purification of abrin from Abrus precatorius. L. Leguminosae. J. Formos. Med. Assoc. 68 : 468-477
Lin, J. Y., Shaw, Y. S., and Tung, T. C. (1971) Studies on the active principle from Abrus precatorius L. Leguminoxal seeds kernels. Toxicon 9 : 97-101
Lin, J. Y., Tserng, K. Y., Chen, C. C., Lin, L. T., and Tung, T. C. (1970) Abrin and ricin : new anti-tumour substances. Nature 227 : 292-293
Ling, K. H., and Tung, T. C. (1948) The oxidative demethylation of monomethyl-L-amino-acids. J. Biol. Chem. 174 : 643-645
Liu, C. L., Tsai, C. C., Lin, S. C., Wang, L. I., Hsu, C. I., Hwang, M. J., and Lin, J. Y. (2000) Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity.
J Biol Chem. 275 : 1897-1901
Lord, J. M. (1985) Precursor of ricin and Ricinus communis agglutinin glycosylation and processing during intracellular transport. Eur. J. Biochem. 146 : 411-416
Lord, J. M. (1985) Synthesis and intracellular transport of lectin and storage protein precursors in endosperm from castor bean. Eur. J. Biochem. 146 : 403-409
Lord, J. M., Roberts, L. M., and Robertus, J. D. (1994) Ricin: structures, mode of action and some current applications. FASEB J. 8 : 201-208
MacConnell, W. P., and Kaplan, N. O. (1980) The role of ethanol extractable proteins from the 80S rat liver ribosome. Biochem Biophys Res Commun. 92 : 46-52
MacConnell, W. P., and Kaplan, N. O. (1982) The activity of the acidic phosphoproteins from the 80 S rat liver ribosome. J. Biol. Chem. 257 : 5359-5366
Makela, O. (1957) Blood group A of human. Ann. Med. Exp. Biol. Fenn. 35 : 11-33
Marinkovich, V. (1964) Purification and characterization of the hemagglutinin present in potatoes. J. Immunol. 93 : 732-738
McGrath, M. S., Huang, K. M., Caldwell, S. E., Gaston, I., Luk, K. C., Wu, P., Ng, V. L., Crowe, S., Daniels, J., Marsh, J., Deinhart, T., Lekas, P. V., Vennari, J. C., Yeung, H. W., and Lifson, J. D. (1989) GLQ233: an inhibitor of human immunodeficiency virus replication in acutely and chronically infected cells of lymphocyte and mononuclear phagocyte lineage. Proc. Natl. Acad. Sci. USA 86 : 2844-2848
Montanaro, L., Sperti, S., Mattioli, A., Testoni, G., and Stripe, F. (1975) Inhibiton by ricin of protein synthesis in vitro. Biochem. J. 146 : 127-131
Montanaro, L., Sperti, S., and Stirpe, F. (1973) Inhibition by ricin of protein synthesis in vitro. Ribosomes as the target of the toxin. Biochem J. 136 : 677-683
Morris, K. N., and Wool, I. G. (1994) Analysis of the contribution of an amphiphilic a-helix to the structure and to the function of ricin A chain. Proc. Natl. Acad. Sci. USA 91 : 7530-7533
Nicolson, G. L., Lacobiere, M., and Hunter, T. R. (1972) Mechanism of cell entry and toxicity of an affinity- purified lectin from Ricinus communis and its differential effects on normal and virus-transformed fibroblasts. Cancer Res. 35 : 144-155
Nolan, R. D., Grasmuk, H., and Dyews, J. (1976) The binding of tritiated elongation-factors 1 and 2 to ribosomes from krebs II mouse ascites-tumor cells. Eur. J. Biochem. 64 : 69-76
Olsnes, S., and Phil, A. (1973) Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis. Biochemistry 12 : 3121-3126
Olsnes, S., Rofsnes, K., Christensen, T. B., and Pihl, A. (1975) Studies on the structures and properties of the lectins from Abrus precatorius and Ricinus communis. Biochim. Biophys. Acta 405 : 1-10
Peter, F., Van, P. N., and Soling, H. D. (1992) Different sorting of Lys-Asp-Glu-Leu proteins in rat liver. J. Biol. Chem. 267 : 10631-10637
Ready, M. P., Adams, R. P., and Robertus, J. D. (1984) Dodecandrin, a new ribosome-inhibiting protein from Phytolacca dodecandra. Biochim. Biophys. Acta 791 : 314-319
Ready, M. P., Brown, D. T., and Robertus, J. D. (1986) Extracellular localization of pokeweed antiviral protein. Proc. Natl. Acad. Sci. USA 83 : 5053-5056
Ready, M. P., Wilson, K., Piatak, M., and Robrtus, J. D. (1984) Ricin-like plant toxins are evolutionarily related to single-chain ribosome-inhibiting proteins from phytolacca. J. Biol. Chem. 259 : 15252-15256
Remacha, M., Jimenez-Diaz, A., Santos, C., Briones, E., Zambrano, R., Rodriguez Gabriel, M. A., Guarinos, E., and Ballesta, J. P. (1995) Proteins P1, P2, and P0, components of the eukaryotic ribosome stalk. New structural and functional aspects. Biochem. Cell Biol. 73 : 959-968
Rich, B. E., and Steitz, J. A. (1987) Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Mol. Cell Biol. 7 : 4065-4074
Robers, W. K., and Selitrennikoff, C. P. (1986) Plant proteins that inactivate foreign ribosomes. Biosci. Reports 6 : 19-29
Roberts, L. M., and Lord, J. M. (1981) The synthesis of Ricinus communis agglutinin : cotranslation and posttranslation modification of agglutinin polypeptides. Eur. J. Biochem. 119 : 31-41
Robrtus, J. D., and Ready, M. P. (1984) Ricin B chain and discoidin I share a common primitive protein fold. J. Biol. Chem. 259 : 13953-13956
Sandvig, K., and Olsnes, S. (1981) Rapid entry of nicked diptheria toxin into cells at low pH. Characterization of the entry process and effect of low pH on the toxin molecule. J. Biol. Chem. 256 : 9068-9076
Sandvig, K., and van Deurs, B. (1992) Toxin-induced cell lysis: protection by 3-methyladenine and cycloheximide. Exp. Cell Res. 200 :253-262
Sandvig, K., Olsnes, S., and Pihl, A. (1976) Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells. J. Biol. Chem. 251 : 3977-3984
Sandvig, K., Prydz, K., Hansen, S. H., and van Deurs, B. (1991) Ricin transport in brefeldin A-treated cells: Correlation between Golgi structure and toxic effect. J. Cell Biol. 115 : 971-981
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
Sharon, N. (1977) Lectins. Sci. Am. 6 : 108-109
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid. Anal. Biochem. 150 : 76-85
Stirpe, F., Barbieri, L., Battelli, M. G., Soria, M., and Lappi, D. A. (1992) Ribosome-inactivating proteins from plants: present status and future prospects. Bio/Technology 10 : 405-412
Stirpe, F., Gasperi-Campani, A., Barbieri, L., Falasca, A., Abbon-danza, A., and Stevens, W. A. (1983) Ribosome-inactivating proteins from the seeds of Saponaria officinalis L. (soapwort), of Agrostemma githago L. (corn cockle) and of Asparagus officinalis L. (asparagus), and from the latex of Hura crepitans L. (sandbox tree). Biochem. J. 216 : 617-625
Stockert, T., Morell, A., and Schernberg, I. (1974) Mammalian hepatic lectin. Science 186 : 365-366
Stripe, F., Legg, R. F., Onyon, L. J., Ziska, P., and Franz, H. (1980) Inhibition of protein synthesis by a toxic lectin from Viscum album L. (mictletoe). Biochem. J. 190 : 843-845
Stripe, F. S., and Barbieri, L. (1986) Ribosome-inactivating proteins up to date. FEBS Lett. 195 : 1-8
Tahirov, T. H., Lu, T. H., Liaw, Y. C., Chen, Y. L., and Lin, J. Y. (1995) Crystal structure of abrin-a at 2.14 A. J. Mol. Biol. 250 : 354-367
Timar, J., McIntosh, D. P., Henry, R., Cumber, A. J., Parnell, G., and Davies, A. J. S. (1991) The effect of ricin B chain on the intracellular trafficking of an A chain immunotoxin. Br. J. Cancer 64 : 655-662
Tomlinson, J. A., Walker, V. M., Flewett, T. H., and Barclay, G. R. (1974) The inhibition of infection by cucumber mosaic virus and influenza virus by extracts from Phytolacca americana. J. Gen. Virol. 22 : 225-232
Treves, A. J., Cohen, I. R., and Feldman, M. S. (1975) Immunotherapy of lethal metastasis of lymphocytes sensitized against tumor cells in vitro. J. Natl. Cancer Inst. Res. 777-780
Tsurugi, K., and Ogata, K. (1985) Evidence for the exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver. J. Biochem. 98 : 1427-1431
Tung, T. C. (1978) Studies on toxic proteins of seeds of Abrus precatorius. J. Formos. Med. Assoc. 77 : 699-705
Tung, T. C., and Liau, M. C. (1960) Studies on the chemical components of the seed of Abrus precatorius. J. Formas. Med. Assoc. 59 : 868-875
Uchiumi, T., Kikuchi, M., and Ogata, K. (1986) Cross-linking study on protein neighborhoods at the subunit interface of rat liver ribosomes with 2-iminothiolane. J. Biol. Chem. 261 : 9663-9667
Uchiumi, T., Kikuchi, M., Terao, K., Iwasaki, K., and Ogata, K. (1986) Cross-linking of elongation factor 2 to rat-liver ribosomal proteins by 2-iminothiolane. Eur. J. Biochem. 156 : 37-48
Uchiumi, T., Kikuchi, M., Terao, K., and Ogata, K. (1985) Cross-linking study on protein topography of rat liver 60 S ribosomal subunits with 2-iminothiolane. J. Biol. Chem. 260 : 5675-5682
Uchiumi, T., Sato, N., Wada, A., and Hachimori, A. (1999) Interaction of the sarcin/ricin domain of 23 S ribosomal RNA with proteins L3 and L6. J. Biol. Chem. 274 : 681-686
Unwin, N., and Henderson, R. (1984) The structure of proteins in biological membranes. Sci. Am. 250 : 78-85
Vater, C. A., Bartle, L. M., Leszyk, J. D., Lambert, J. M., and Goldmacher, V. S. (1995) Ricin A chain can be chemical cross-linked to mammalian ribosomal proteins L9 and L10e. J. Biol. Chem. 270 : 12933-12940
Veldman, G. M., Klootwijk, J., de Regt, V. C. H. F., Planta, R. J., Branlornt, C., Krol, A., and Ebel, J. P.(1981) The primary and secondary structure of yeast 26 S RNA. Nucleic Acids Res. 9 : 6935-6952
Verschoor, A., Srivastava, S., Grassucci, R., and Frank, J. (1996) Native 3D structure of eukaryotic 80S ribosome: morphological homology with E. coli 70S ribosome. J. Cell. Biol. 133 : 495-505
Walter, P., Gilmore, R., and Blobel, G. (1984) Protein translocation across the endoplasmic reticulum. Cell 38 : 5-16
Wang, Y. X., Neamati, N., Jacob, J., Kaufman, J. D., Huang, P. L., Huang, P. L., Winslow, H. E., Pommier, Y., Wingfield, P. T., Lee-Huang, P., Bax, A., and Torchia, D. A. (1999) Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions. Cell 99 : 433-442
Wawrzhycake, E. J., Zangemeister-Wittke, V., Wiabel, R., Henry, R. V., Parnell, G. D., Cumber, A. J., Jones, M., and Stahel, R. A. (1992) Molecular and biological properties of an abrin A chain immuntoxin designed for therapy of human small cell lung cancer. Br. J. Cancer 66 : 361-366
Weston, S. A., Tucker, A. D., Thatcher, D. R., Derbyshier, D. J., and Pauptit, R. A. (1994) X-ray structure of recombinant ricin A-chain at 1.88 A resolution. J. Mol. Biol. 244 : 410-422
Wool, I. G., Chan, Y. L., and Gluck, A. (1995) Structure and evolution of mammalian ribosomal proteins. Biochem. Cell Biol. 73 : 933-947
Yamaizumi, M., Uchida, T., and Okada, Y. (1979) Macromolecules can penetrate the host cell membrane during the early period of incubation with HVJ (sendai virus). Virology 95 : 218-221
Yeung, H. W., Li, W. W., Feng, Z., Barbieri, L., and Stirpe, F. (1988) Trichosanthin, a-momorcharin and b-momorcharin : identity of abortifacient and ribosome-inactivating proteins. Intl. J. Pept. Protein Res. 31 : 265-268
Yoshida, T., Chen, C., Zang, M., and Wu, H. C. (1991) Disruption of Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin and Pseudomonas toxin. Exp. Cell Res. 192 : 389-395
Yoshitake, S., Funatsu, G., and Funatsu, M. (1978) Isolation and sequences of peptic peptides, and the complete sequence of Ile chain of ricin-D. Agric. Biol. Chem. 42 : 1267-1274
Zinker, S., and Warner, J. R. (1976) The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins. J. Biol. Chem. 251 : 1799-1807