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Research Article

Functional Modification of a 21-Kilodalton G Protein when ADP-Ribosylated by Exoenzyme C3 of Clostridium botulinum

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Pages 418-426 | Received 09 Sep 1987, Accepted 22 Oct 1987, Published online: 31 Mar 2023

Literature Cited

  • Aktories, K., M. Barmann, I. Ohishi, S. Tsuyama, K. H. Jakobs, and E. Habermann. 1986. Botulinum C2 toxin ADP-ribosylates actin. Nature (London) 322:390-392.
  • Aktories, K., U. Weller, and G. S. Chatwal. 1987. Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin. FEBS Lett. 212:109-113.
  • Bar-Sagi, D., and J. R. Feramisco. 1985. Microinjection of the ras oncogene protein into PC12 cells induces morphological differentiation. Cell 42:841-848.
  • Birchmeier, C., D. Brock, and M. Wigler. 1985. ras proteins can induce meiosis in Xenopus oocytes. Cell 43:615-621.
  • Burnette, W. N. 1981. “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195-203.
  • Chardin, P., and A. Tavitian. 1986. The ral gene: a new ras-related gene isolated by the use of a synthetic probe. EMBO J. 5:2203-2208.
  • Cleveland, D. W., S. G. Fisher, M. W. Kirschner, and U. K. Laemmli. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252:1102-1106.
  • Eklund, M. W., F. T. Poyski, S. M. Feed, and C. A. Smith. 1971. Bacteriophage and the toxigenicity of Clostridium botulinum type C. Science 172:480-482.
  • Evans, T., M. L. Brown, E. D. Fraser, and J. K. Northup. 1986. Purification of the major GTP-binding proteins from human placental membranes. J. Biol. Chem. 261:7052-7059.
  • Feramisco, J. R., M. Gross, T. Kamata, M. Rosenberg, and R. W. Sweet. 1984. Microinjection of the oncogene form of the human H-ras T-24 protein results in rapid proliferation of quiescent cells. Cell 38:109-117.
  • Furth, M. E., L. J. Davis, B. Fleudelys, and E. M. Scolnik. 1982. Monoclonal antibodies to the p21 products of the transforming gene of Harvey murine sarcoma virus and of the cellular ras gene family. J. Virol. 43:294-304.
  • Gibbs, J. B., I. S. Sigal, M. Poe, and E. M. Scolnick. 1984. Intrinsic GTPase activity distinguishes normal and oncogenic ras p21 molecules. Proc. Natl. Acad. Sci. USA 81:5704-5708.
  • Gibbs, J. B., I. S. Sigal, and E. M. Scolnick. 1985. Biochemical properties of normal and oncogenic ras p21. Trends Biochem. Sci. 10:350-353.
  • Gill, D. M., and R. Meren. 1983. A second guanyl nucleotide- binding site associated with adenylate cyclase. J. Biol. Chem. 258:11908-11914.
  • Gill, D. M., and A. M. Pappenheimer, Jr. 1971. Structurefunction relationships in diphtheria toxin. J. Biol. Chem. 246:1492-1495.
  • Gilman, A. G. 1984. G proteins and dual control of adenylate cyclase. Cell 36:577-579.
  • Greene, L. A., and A. S. Tischler. 1982. PC12 pheochromocytoma cultures in neurobiological research. Adv. Cell. Neurobiol. 3:373-414.
  • Hattori, S., T. Yamashita, T. D. Copeland, S. Oroszlan, and T. Y. Shih. 1986. Reactivity of a sulfhydryl group of the ras oncogene product p21 modulated by GTP binding. J. Biol. Chem. 261:14582-14586.
  • Kahn, R. A., and A. G. Gilman. 1986. The protein factor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP-binding protein. J. Biol. Chem. 261:7906-7911.
  • Lowe, D. G., D. J. Capon, E. Delwart, A. Y. Sakaguchi, S. L. Naylor, and D. V. Goeddel. 1987. Structure of the human and murine R-ras genes, novel genes closely related to ras protooncogenes. Cell 48:137-146.
  • Madaule, P., and R. Axel. 1985. A novel ras-related gene family. Cell 41:31-40.
  • Miyazaki, S., M. Iwasaki, and G. Sakaguchi. 1977. Clostridium botulinum type D toxin: purification, molecular structure, and some immunological properties. Infect. Immun. 17:395-401.
  • Oguma, K., T. Yamaguchi, K. Sudou, N. Yokosawa, and Y. Fujikawa. 1986. Biochemical classification of Clostridium botulinum type C and D strains and their nontoxigenic derivatives. Appl. Environ. Microbiol. 51:256-260.
  • Ohashi, Y., and S. Narumiya. 1987. ADP-ribosylation of a Mr 21,000 membrane protein by type D botulinum toxin. J. Biol. Chern. 262:1430-1433.
  • Ohishi, I., M. Iwasaki, and G. Sakaguchi. 1980. Purification and characterization of two components of botulinum C2 toxin. Infect. Immun. 30:668-673.
  • Oka, J., K. Ueda, and O. Hayaishi. 1978. Snake venom phosphodiesterase: simple purification with blue Sepharose and its application to poly (ADP-ribose) study. Biochem. Biophys. Res. Commun. 80:841-848.
  • Okada, C. Y., and M. Rechsteiner. 1982. Introduction of macromolecules into cultured mammalian cells by osmotic lysis of pinocytotic vesicles. Cell 29:33-41.
  • Roa, M., and P. Boquet. 1985. Interaction of tetanus toxin with lipid vesicles at low pH. J. Biol. Chern. 260:6827-6835.
  • Schmitt, H. D., P. Wagner, E. Pfaff, and D. Gallwitz. 1986. The ras-related YPT1 gene product in yeast: a GTP-binding protein that might be involved in microtubule organization. Cell 47:401-412.
  • Shih, T. Y., M. O. Weeks, P. Gruss, R. Dhar, S. Oroszlan, and E. M. Scolnick. 1982. Identification of a precursor in the biosynthesis of the p21 transforming protein of Harvey murine sarcoma virus. J. Virol. 42:253-261.
  • Sigal, I. S., J. B. Gibbs, J. S. d’Alonzo, and E. M. Scolnick. 1986. Identification of effector residues and a neutralizing epitope of Ha-ras-encoded p21. Proc. Natl. Acad. Sci. USA 83:4725-4729.
  • Simpson, L. L. 1986. Molecular pharmacology of botulinum toxin and tetanus toxin. Annu. Rev. Pharmacol. Toxicol. 26:427-453.
  • Stacey, D. W., and H.-F. Kung. 1984. Transformation of NIH 3T3 cells by microinjection of Ha-ras p21 protein. Nature (London) 310:508-511.
  • Tamir, A., and A. M. Tolkovsky. 1985. Transient states of adenylate cyclase in brain membranes. J. Neurochem. 44:1006-1013.
  • Yin, H. H., and R. D. Berlin. 1975. The relation of endogenous adenosine cyclic 3′:5′-monophosphate to the antagonistic effects of adenosine and colchicine on cell shape. J. Cell. Physiol. 85:635-642.

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