Evidence that Arg-295, Glu-378, and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin

FEBS Letters

Volumn 395, Issue 2-3, 1996, Pages 191-194

  Perelle, Sylvie ^a   Domenighini, Mario ^b   Popoff, Michel R ^a  

^a INSTITUT PASTEUR   (France)

^b Instituto Ricerche Immunobiol Siena   (Italy)

Author keywords

ADP ribosylating toxin; C. difficile ADP ribosyltransferase; C. spiroforme toxin; C3 enzyme; Clostridium perfringes; Iota toxin

Indexed keywords

CHOLERA TOXIN; CLOSTRIDIUM TOXIN; ESCHERICHIA COLI ENTEROTOXIN; PERTUSSIS TOXIN;

AMINO ACID COMPOSITION; ARTICLE; CLOSTRIDIUM PERFRINGENS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ESCHERICHIA COLI; GENE CONSTRUCT; MUTANT; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

CLOSTRIDIUM; CLOSTRIDIUM DIFFICILE; CLOSTRIDIUM PERFRINGENS; CLOSTRIDIUM PERFRINGES; CLOSTRIDIUM SPIROFORME; ESCHERICHIA COLI;

EID: 0030597057     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(96)01035-6     Document Type: Article

References (23)

1. [1] Domenighini, M., Magagnoli, C., Pizza, M. and Rappuoli, R. (1994) Mol. Microbiol. 14, 41-50.
2. [2] Just, I., Schallehn, G. and Aktories, K. (1992) Biochem. Biophys. Res. Commun. 183, 931-936.
3. [3] Just, I., Mohr, C., Schallehn, G., Menard, L., Didsbury, J.R., Vandekerckhove, J., Van Damme, J. and Aktories, K. (1992) J. Biol. Chem. 267, 10274-10280.
4. [4] Inoue, S., Sugai, M., Murooka, Y., Paik, S.Y., Hong, Y.M., Ohgai, H. and Suginaka, H. (1991) Biochem. Biophys. Res. Commun. 174, 459-464.
5. [5] Aktories, K., Bärmann, M., Ohishi, I., Tsuyama, S., Jakobs, K.H. and Habermann, E. (1986) Nature 322, 390-392.
6. [6] Popoff, M.R. and Boquet, P. (1988) Biochem. Biophys. Res. Commun. 152, 1361-1368.
7. [7] Popoff, M.R., Rubin, E.J., Gill, D.M. and Boquet, P. (1988) Infect. Immun. 56, 2299-2306.
8. [8] Simpson, L.L., Stiles, B.G., Zepeda, H.H. and Wilkins, T.D. (1987) Infect. Immun. 55, 118-122.
9. [9] Domenighini, M., Pizza, M. and Rappuoli, R. (1995) in: Bacterial Toxins and Virulence Factors in Disease (Moss, J. et al. eds.) pp. 59-80, Dekker, New York.
10. [10] Jung, M., Just, I., Van Damme, J., Vandekerckhove, J. and Aktories, K. (1993) J. Biol. Chem. 268, 23215-23218.
11. [11] Saito, Y., Nemoto, Y., Ishizaki, T., Watanabe, N., Morii, N. and Narumiya, S. (1995) FEBS Lett. 371, 105-109.
12. [12] Stiles, B.G. and Wilkins, T.D. (1986) Infect. Immun. 54, 683-688.
13. [13] Stiles, B.G. and Wilkins, T.D. (1986) Toxicon 24, 767-773.
14. [14] Vandekerckhove, J., Schering, B., Bärmann, M. and Aktories, K. (1987) FEBS Lett. 255, 48-52.
15. [15] Perelle, S., Gibert, M., Boquet, P. and Popoff, M.R. (1993) Infect. Immun. 61, 5147-5156.
16. [16] Perelle, S., Gibert, M., Boquet, P. and Popoff, M.R. (1995) Infect. Immun. 63, 4967.
17. [17] Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
18. [18] Popoff, M.R., Milward, F.W., Bancillon, B. and Boquet, P. (1989) Infect. Immun. 57, 2462-2469.
19. [19] Van Damme, J., Jung, M., Hofmann, F., Just, I., Vandekerckhove, J. and Aktories, K. (1996) FEBS Lett. 380, 291-295.
20. [20] Lobet, Y., Cluff, C.W. and Cieplak, W. (1991) Infect. Immun. 59, 2870-2879.
21. [21] Takada, T., Iida, K. and Moss, J. (1995) J. Biol. Chem. 270, 541-544.
22. [22] Aktories, K. (1994) Mol. Cel. Biochem. 138, 167-176.
23. [23] Considine, R.V. and Simpson, L.L. (1991) Toxicon 29, 913-936.