Identification of shallow and deep membrane-penetrating forms of diphtheria toxin T domain that are regulated by protein concentration and bilayer width

Journal of Biological Chemistry

Volumn 272, Issue 40, 1997, Pages 25091-25098

  Wang, Yang ^a   Malenbaum, Susan E ^a   Kachel, Kelli ^a   Zhan, Hangjun ^b,c   John Collier, R ^b   London, Erwin ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c Arris Pharmaceuticals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIPHTHERIA TOXIN; PHOSPHOLIPID;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; BILAYER MEMBRANE; CORYNEBACTERIUM DIPHTHERIAE; FLUORESCENCE; LIPID BILAYER; MEMBRANE VESICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SITE DIRECTED MUTAGENESIS;

BORON COMPOUNDS; CLONING, MOLECULAR; CYSTEINE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIPHTHERIA TOXIN; ESCHERICHIA COLI; FLUORESCENT DYES; HYDROGEN-ION CONCENTRATION; KINETICS; LIPID BILAYERS; MODELS, STRUCTURAL; MUTAGENESIS, SITE-DIRECTED; PHOSPHATIDYLCHOLINES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPIN LABELS; STRUCTURE-ACTIVITY RELATIONSHIP;

CORYNEBACTERIUM DIPHTHERIAE; STAPHYLOCOCCUS PHAGE 3A;

EID: 0030803672     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.40.25091     Document Type: Article

References (33)

1. Collier, R. J. (1982) in ADP-Ribosylation Reactions: Biology and Medicine (Hayashi, O., and Ueda, K., eds.) pp. 575-592, Academic Press, Inc., New York
2. Choe, S., Bennett, M. J., Fuji, G., Curmi, P. M. G., Kantardjieff, K. A., Collier, R. J., and Eisenberg, D. (1992) Nature 357, 216-222
3. Bennett, M. J., and Eisenberg, D. (1994) Protein Sci. 3, 1464-1475
4. Bennett, M. J., Choe, S., and Eisenberg, D. (1994) Protein Sci. 3, 1444-1463
5. Bell, C. E., and Eisenberg, D. (1997) Biochemistry 36, 481-488
6. London, E. (1992) Biochim. Biophys. Acia 1113, 25-51
7. London, E. (1992) Mol. Microbiol. 6, 3277-3282
8. Cabiaux, V., Quertenmont, P., Conrath, K., Brasseur, R., Capiau, C., and Ruysschaert, J.-M. (1994) Mol. Microbiol. 11, 43-50
9. Zhan, H., Choe, S., Huynh, P. D., Finkelstein, A., Eisenberg, D., and Collier, R. J. (1994) Biochemistry 33, 11254-11263
10. Mindell, J. A., Zhan, H., Huynh, P. D., Collier, R. J., and Finkelstein, A. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 5272-5276
11. Silverman, J. A., Mindell, J. A., Zhan, H., Finkelstein, A., and Collier, R. J. (1994) J. Membr. Biol. 137, 17-28
12. Mindell, J. A., Silverman, J. A., Finkelstein, A., and Collier, R. J. (1994) J. Membr. Biol. 137, 29-44
13. Mindell, J. A., Silverman, J. A., Finkelstein, A., and Collier, R. J. (1994) J. Membr. Biol. 137, 45-57
14. Zhan, H., Oh, K. J., Shin Y.-K., Hubbell, W. L., and Collier, R. J. (1995) Biochemistry 34, 4856-4863
15. Oh, K. J., Zhan, H., Cui, C., Hideg, K., Collier, R. J., and Hubbell, W. L. (1996) Science 273, 810-812
16. Asuncion-Punzalan, E., and London, E. (1995) Biochemistry 34, 11460-11466
17. Jiang, J. X., Abrams, F. S., and London, E. (1991) Biochemistry 30, 3857-3864
18. Chattopadhyay, A., and London, E. (1987) Biochemistry 26, 39-45
19. Abrams, F. S., and London, E. (1993) Biochemistry 32, 10826-10831
20. Blewitt, M. G., Chung, L. A., and London, E. (1985) Biochemistry 24, 5458-5464
21. Jiang, J. X., and London, E. (1990) J. Biol. Chem. 265, 8636-8641
22. Tortorella, D., Sesardic, D., Dawes, D. S., and London, E. (1995) J. Biol. Chem. 270, 27439-27445
23. Ren, J., Lew, S., Wang, Z., and London, E. (1997) Biochemistry 36, 10213-10220
24. Lewis, B. A., and Engelman, D. M. (1983) J. Mol. Biol. 166, 211-217
25. Caffrey, M., and Feigenson, G. W. (1981) Biochemistry 20, 1949-1961
26. Johannsson, A., Keightley, C. A., Smith G. A., Richards, C. D., Hesketh, T. R., and Metcalfe, J. C. (1981) J. Biol. Chem. 256, 1643-1650
27. Haydon, D. A., Hendry, B. M., Levinson, S. R., and Requena, J. (1977) Biochim. Biophys. Acta 470, 17-34
28. Milne, J. C. Furlong, D., Hanna, P. C., Wall, J. S., and Collier, R. J. (1994) J. Biol. Chem. 269, 20607-20612
29. Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996) Science 274, 1859-1866
30. Walker, B., Krishnasastry, M., Zorn, L., and Bayley, H. (1992) J. Biol. Chem. 267, 21782-21786
31. Kagan, B. L., Finkelstein, A., and Colombini, M. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4950-4954
32. Papini, E., Schiavo, G., Tomasi, M., Colombatti, M., Rappuoli, R., and Montecucco, C., (1987) Eur. J. Biochem. 169, 637-644
33. Zalman, L. S., and Wisnieski, B. J. (1984) Proc. Natl. Acad. Sci. U. S. A. 81, 3341-3345