Khursigara, Cezar M., De Crescenzo, Gregory, Pawelek, Peter D. and Coulton, James W. (2004) Enhanced Binding of TonB to a Ligand-loaded Outer Membrane Receptor: ROLE OF THE OLIGOMERIC STATE OF TonB IN FORMATION OF A FUNCTIONAL FhuA·TonB COMPLEX. Journal of Biological Chemistry, 279 (9). pp. 7405-7412. ISSN 0021-9258
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Official URL: http://www.jbc.org/cgi/content/abstract/279/9/7405
Abstract
The ferric hydroxymate uptake (FhuA) receptor from Escherichia coli facilitates transport of siderophores ferricrocin and ferrichrome and siderophore-antibiotic conjugates such as albomycin and rifamycin CGP 4832. FhuA is also the receptor for phages T5, T1, 80, UC-1, for colicin M and for the antimicrobial peptide microcin MccJ21. Energy for transport is provided by the cytoplasmic membrane complex TonB·ExbB·ExbD, which uses the proton motive force of the cytoplasmic membrane to transduce energy to the outer membrane. To accomplish energy transfer, TonB contacts outer membrane receptors. However, the stoichiometry of TonB· receptor complexes and their sites of interaction remain uncertain. In this study, analyses of FhuA interactions with two recombinant TonB proteins by analytical ultracentrifugation revealed that TonB forms a 2:1 complex with FhuA. The presence of the FhuA-specific ligand ferricrocin enhanced the amounts of complex but is not essential for its formation. Surface plasmon resonance experiments demonstrated that FhuA·TonB interactions are multiple and have apparent affinities in the nanomolar range. TonB also possesses two distinct binding regions: one in the C terminus of the protein, for which binding to FhuA is ferricrocin-independent, and a higher affinity region outside the C terminus, for which ferricrocin enhances interactions with FhuA. Together these experiments establish that FhuA·TonB interactions are more intricate than originally predicted, that the TonB·FhuA stoichiometry is 2:1, and that ferricrocin modulates binding of FhuA to TonB at regions outside the C-terminal domain of TonB.
Divisions: | Concordia University > Faculty of Arts and Science > Chemistry and Biochemistry |
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Item Type: | Article |
Refereed: | Yes |
Authors: | Khursigara, Cezar M. and De Crescenzo, Gregory and Pawelek, Peter D. and Coulton, James W. |
Journal or Publication: | Journal of Biological Chemistry |
Date: | February 2004 |
ID Code: | 6343 |
Deposited By: | KUMIKO VEZINA |
Deposited On: | 14 Sep 2009 19:43 |
Last Modified: | 18 Jan 2018 17:28 |
References:
Boulanger, P., le Maire, M., Bonhivers, M., Dubois, S., Desmadril, M., and Letellier, L. (1996) Biochemistry 35, 14216–14224Braun, V., Hantke, K., and Köster, W. (1998) in Metal Ions in Biological Systems (Sigel, A., and Sigel, H., eds) Vol. 35, pp. 67–145, Marcel Dekker, Inc., New York
Braun, V., and Braun, M. (2002) Curr. Opin. Microbiol. 5, 194–201
Buchanan, S. K., Smith, B. S., Venkatramani, L., Xia, D., Esser, L., Palnitkar, M., Chakraborty, R., van der Helm, D., and Deisenhofer, J. (1999) Nat. Struct. Biol. 6, 56–63
Cadieux, N., and Kadner, R. J. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 10673–10678
Cadieux, N., Bradbeer, C., and Kadner, R. J. (2000) J. Bacteriol. 182, 5954–5961
Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535–27540
Chimento, D. P., Kadner, R. J., and Wiener, M. C. (2003) J. Mol. Biol. 332, 999–1014
Chimento, D. P., Mohanty, A. K., Kadner, R. J., and Wiener, M. C. (2003) Nat. Struct. Biol. 10, 394–401
De Crescenzo, G., Grothe, S., Lortie, R., Debanne, M. T., and O'Connor-McCourt, M. (2000) Biochemistry 39, 9466–9476
De Crescenzo, G., Grothe, S., Zwaagstra, J., Tsang, M., and O'Connor-McCourt, M. D. (2001) J. Biol. Chem. 276, 29632–29643
Evans, J. S., Levine, B. A., Trayer, I. P., Dorman, C. J., and Higgins, C. F. (1986) FEBS Lett. 208, 211–216
Ferguson, A. D., Coulton, J. W., Diederichs, K., and Welte, W. (2001) in Handbook of Metalloproteinsin (Messerschmidt, A., Huber, R., Poulos T., and Wieghardt, K., eds) pp. 834–849, John Wiley & Sons, Ltd., Chichester
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., and Welte, W. (1998) Science 282, 2215–2220
Ferguson, A. D., Chakraborty, R., Smith, B. s., Esser, L., van der Helm, D., and Deisenhofer, J. (2002) Science 295, 1715–1719
Ferguson, A. D., Breed, J., Diederichs, K., Welte, W., and Coulton, J. W. (1998) Protein Sci. 7, 1636–1638
Gunter, K., and Braun, V. (1990) FEBS Lett. 274, 85–88
Johnsson, B., Lofas, S., and Lindquist, G. (1991) Anal. Biochem. 198, 268–277
Larsen, R. A., Letain, T. E., and Postle, K. (2003) Mol. Microbiol. 49, 211–218
Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., and Moras, D. (1998) Cell 95, 771–778
Moeck, G. S., Tawa, P., Xiang, H., Ismail, A. A., Turnbull, J. L., and Coulton, J. W. (1996) Mol. Microbiol. 22, 459–471
Moeck, G. S., and Coulton, J. W. (1998) Mol. Microbiol. 28, 675–681
Moeck, G. S., Coulton, J. W., and Postle, K. (1997) J. Biol. Chem. 272, 28391–28397
Moeck, G. S., and Letellier, L. (2001) J. Bacteriol. 183, 2755–2764
Perkins, S. J. (1986) Eur. J. Biochem. 157, 169–180
Postle, K., and Kadner, R. J. (2003) Mol. Microbiol. 49, 869–882
Rich, R. L., and Myszka, D. G. (2000) Curr. Opin. Biotechnol. 11, 54–61
Sauter, A., Howard, S. P., and Braun, V. (2003) J. Bacteriol. 185, 5747–5754
Schoffler, H., and Braun, V. (1989) Mol. Gen. Genet. 217, 378–383
Schuck, P. (2000) Biophys. J. 78, 1606–1619
Skare, J. T., Ahmer, B. M., Seachord, C. L., Darveau, R. P., and Postle, K. (1993) J. Biol. Chem. 268, 16302–16308
Zhai, Y. F., Heijne, W., and Saier, M. H., Jr. (2003) Biochim. Biophys. Acta 1614, 201–210
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