Role of Arginine 180 and Glutamic Acid 177 of Ricin Toxin A Chain in Enzymatic Inactivation of Ribosomes

LITERATURE CITED

• Baenziger, J., and D. Fiete. 1979. Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides. J. Biol. Chem. 254:9795–9799.
   PubMed Web of Science ®Google Scholar
• Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   PubMed Web of Science ®Google Scholar
• Bradley, J., M. Piatak, J. Lane, and P. McGuire. 1989. Site-directed mutagenesis at amino terminus of recombinant ricin A chain. Int. J. Peptide Protein Res. 34:2–5.
   PubMedGoogle Scholar
• Dunn, B., and T. Bruice. 1973. Physical organic models for mechanism of lysozyme action. Adv. Enzymol. 37:1–60.
   PubMedGoogle Scholar
• Eiklid, K., S. Olsnes, and A. Phil. 1980. Entry of lethal doses of abrin, ricin, and modeccin into the cytosol of HeLa cells. Exp. Cell Res. 126:321–326.
   PubMed Web of Science ®Google Scholar
• Endo, Y., K. Mitsui, M. Motizuki, and K. Tsurugi. 1987. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. J. Biol. Chem. 262:5908–5912.
   PubMed Web of Science ®Google Scholar
• Enghild, J., I. Thogersen, P. Roche, and S. Pizzo. 1989. A conserved region in alpha-macroglobulins participates in binding to the mammalian alpha-macroglobulin receptor. Biochemistry 28:1406–1412.
   PubMedGoogle Scholar
• Frankel, A., D. Schlossman, P. Welsh, A. Hertler, D. Withers, and S. Johnston. 1989. Selection and characterization of mutants of ricin toxin A chain in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:415–420.
   Google Scholar
• Goff, C. 1974. Chemical structure of a modification of the Escherichia coli ribonucleic acid polymerase alpha polypeptides induced by bacteriophage T4 infection. J. Biol. Chem. 249:6181–6190.
   PubMed Web of Science ®Google Scholar
• Holmes, D., and M. Quigley. 1981. A rapid boiling method for the preparation of bacterial plasmids. Anal. Biochem. 114:193–197.
   PubMed Web of Science ®Google Scholar
• Hovde, C., S. Calderwood, J. Mekalanos, and R. Collier. 1988. Evidence that glutamic acid 167 is an active site residue of Shiga-like toxin I. Proc. Natl. Acad. Sci. USA 85:2568–2572.
   PubMed Web of Science ®Google Scholar
• Ingram, V. 1957. Gene mutations in human hemoglobin: the chemical difference between normal and sickle cell hemoglobin. Nature (London) 180:326–328.
   PubMed Web of Science ®Google Scholar
• Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Johnston, M., and R. W. Davis. 1984. Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cer- evesiae. Mol. Cell. Biol. 4:1440–1448.
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• May, M., M. Hartley, L. Roberts, P. Krieg, R. Osborn, and J. Lord. 1989. Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides. EMBO J. 8:301–308.
   PubMed Web of Science ®Google Scholar
• Mentch, F., D. Parkin, and V. Schramm. 1987. Transition-state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator. Biochemistry 26:921–930.
   PubMedGoogle Scholar
• Montesano, L., D. Cawley, and H. Herschman. 1982. Disuccin- imidyl suberate cross-linked ricin does not inhibit cell-free protein synthesis. Biochem. Biophys. Res. Commun. 109:7–13.
   PubMedGoogle Scholar
• Montfort, W., J. Villafranca, A. Monzingo, S. Ernst, B. Katzin, E. Rutenber, N. Xuong, R. Hamlin, and J. Robertus. 1987. The 3-dimensional structure of ricin at 2.8 Angstroms. J. Biol. Chem. 262:5398–5403.
   PubMed Web of Science ®Google Scholar
• Moskaluk, C., and D. Bastia. 1988. Interaction of bovine papillomavirus type 1 E2 transcriptional control protein with the virus enhancer: purification of the DNA-binding domain and analysis of its contact points with DNA. J. Virol. 62:1925–1931.
   PubMedGoogle Scholar
• Olsnes, S., and A. Pihl. 1972. Treatment of abrin and ricin with beta-mercaptoethanol. Opposite effects on their toxicity in mice and their ability to inhibit protein synthesis. FEBS Lett. 28:48–50.
   PubMed Web of Science ®Google Scholar
• Ready, M., B. Katzin, and J. Robertus. 1988. Ribosome-inhibiting proteins, retroviral reverse transcriptases, and RNase H share common structural elements. Proteins 3:53–59.
   PubMedGoogle Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Schlossman, D., D. Withers, P. Welsh, A. Alexander, J. Robertus, and A. Frankel. 1989. Role of glutamic acid 177 of ricin toxin A chain in enzymatic inactivation of ribosomes. Mol. Cell. Biol. 9:5012–5021.
   PubMedGoogle Scholar
• Sundan, A., G. Evensen, E. Hornes, and A. Mathiesen. 1989. Isolation and in vitro expression of the ricin A-chain gene: effect of deletions on biological activity. Nucleic Acids Res. 17:1717–1732.
   PubMedGoogle Scholar
• Watanabe, K., and G. Funatsu. 1987. Interaction of Cibacron blue F3GA and polynucleotides with ricin A-chain, 60S ribosomal subunit-inactivating protein. Biochim. Biophys. Acta 914:177–184.
   PubMedGoogle Scholar