Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12

Molecular Microbiology

Volumn 22, Issue 3, 1996, Pages 459-471

  Moeck, Gregory S ^a   Tawa, Paul ^a   Xiang, Hui ^a   Ismail, Ashraf A ^b   Turnbull, Joanne L ^c   Coulton, James W ^a  

^a MCGILL UNIVERSITY   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c Gina Cody School of Engineering and Computer Science   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

FERRICHROME; IRON; MEMBRANE RECEPTOR; OUTER MEMBRANE PROTEIN;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI K 12; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION;

ESCHERICHIA; ESCHERICHIA COLI K12;

EID: 0029836552     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1996.00112.x     Document Type: Article

References (65)

1. Aldema, M.L., McMurry, L.M., Walmsley, A.R., and Levy, S.B. (1996) Purification of the Tn10-specified tetracycline efflux antiporter TetA in a native state as a polyhistidine fusion protein. Mol Microbiol 19: 187-195.
2. Anton, M., and Heller, K.J. (1993) The wild-type allele of tonB in Escherichia coli is dominant over the tonB1 allele, encoding TonBQ160K, which suppresses the btuB451 mutation. Mol Gen Genet 239: 371-377.
3. Bäumler, A.J., and Hantke, K. (1992) Ferrioxamine uptake in Yersinia enterocolitica: characterization of the receptor protein FoxA. Mol Microbiol 6: 1309-1321.
4. Bell, P.E., Nau, C.D., Brown, J.T., Konisky, J., and Kadner, R.J. (1990) Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J Bacteriol 172: 3826-3829.
5. Bonhivers, M., Ghazi, A., Boulanger, P., and Letellier, L. (1996) FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. EMBO J 15: 1850-1856.
6. Braun, V. (1995) Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol Rev 16: 295-307.
7. Braun, V., Frenz, J., Hantke, K., and Schaller, K. (1980) Penetration of colicin M into cells of Escherichia coli. J Bacteriol 142: 162-168.
8. Braun, V., Killmann, H., and Benz, R. (1994) Energy-coupled transport through the outer membrane of Escherichia coli: small deletions in the gating loop convert the FhuA transport protein into a diffusion channel. FEBS Lett 346: 59-64.
9. Carmel, G., and Coulton, J.W. (1991) Internal deletions in the FhuA receptor of Escherichia coli K-12 define domains of ligand interactions. J Bacteriol 173: 4394-4403.
10. Carmel, G., Hellstern, D., Henning, D., and Coulton, J.W. (1990) Insertion mutagenesis of the gene encoding the ferrichrome-iron receptor of Escherichia coli K-12. J Bacteriol 172: 1861-1869.
11. Compton, L.A., and Johnson, Jr, W.C. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal Biochem 155: 155-167.
12. Coulton, J.W., Mason, P., Cameron, D.R., Carmel, G., Jean, R., and Rode, H.N. (1986) Protein fusions of β-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12. J Bacteriol 165: 181-192.
13. Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., and Rosenbusch, J.P. (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358: 727-733.
14. Eisele, J.-L., and Rosenbusch, J.P. (1990) In vitro folding and oligomerization of a membrane protein. Transition of bacterial porin from random coil to native conformation. J Biol Chem 265: 10217-10220.
15. Günter, K., and Braun, V. (1990) In vivo evidence for FhuA outer membrane receptor interaction with the TonB inner membrane protein of Escherichia coli. FEBS Lett 274: 85-88.
16. Härle, C., Kim, I., Angerer, A., and Braun, V. (1995) Signal transfer through three compartments: transcription initiation of the Escherichia coli ferric citrate transport system from the cell surface. EMBO J 14: 1430-1438.
17. Hancock, R.E.W., and Braun, V. (1976) Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi 80 to Escherichia coli. J Bacteriol 125: 409-415.
18. Hantke, K. (1981) Regulation of ferric iron transport in Escherichia coli K-12: isolation of a constitutive mutant. Mol Gen Genet 182: 288-292.
19. Hantke, K., and Braun, V. (1976) A function common to iron-enterochelin transport and action of colicins B, I, V in Escherichia coli. FEBS Lett 59: 277-281.
20. Hantke, K., and Braun, V. (1978) Functional interaction of the tonA/tonB receptor system in Escherichia coli. J Bacteriol 135: 190-197.
21. Heller, K., Kadner, R.J., and Günter, K. (1988) Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli. Gene 64: 147-153.
22. Higgins, C.F. (1992) ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8: 67-113.
23. Higgins, C.F. (1995) The ABC of channel regulation. Cell 82: 693-696.
24. Hoffmann, H., Fischer, E., Kraut, H, and Braun, V. (1986a) Preparation of the FhuA (TonA) receptor protein from cell envelopes of an overproducing strain of Escherichia coli K-12. J Bacteriol 166: 404-411.
25. Hoffmann, H., Fischer, E., Schwarz, H., and Braun, V. (1986b) Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane. Arch Microbiol 145: 334-341.
26. Ingham, C., Buechner, M., and Adler, J. (1990) Effect of outer membrane permeability on chemotaxis in Escherichia coli. J Bacteriol 172: 3577-3583.
27. Johnson, Jr, W.C. (1990) Protein secondary structure and circular dichroism: a practical guide. Proteins: Struct Funct Genet 7: 205-214.
28. Kadner, R.J., and Heller, K.J. (1995) Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function. J Bacteriol 177: 4829-4835.
29. Killmann, H., and Braun, V. (1994) Energy-dependent receptor activities of Escherichia coli K-12: mutated TonB proteins alter FhuA receptor activities to phages T5, T1, phi 80 and to colicin M. FEMS Microbiol Lett 119: 71-76.
30. Killmann, H., Benz, R., and Braun, V. (1993) Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli. EMBO J 12: 3007-3016.
31. Killmann, H., Videnov, G., Jung, G., Schwarz, H., and Braun, V. (1995) Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and phi 80 and colicin M bind to the gating loop of FhuA. J Bacteriol 177: 694-698.
32. Klebba, P.E., Rutz, J.M, Liu, J., and Murphy, C.K. (1993) Mechanisms of TonB-catalysed iron transport through the enteric bacterial cell envelope. J Bioenergetics Biomemb 25: 603-611.
33. Klug, C.S., Su, W., Liu, J., Klebba, P.E., and Feix, J.B. (1995) Denaturant unfolding of the ferric enterobactin receptor and ligand-induced stabilization studied by site-directed spin labeling. Biochemistry 34: 14230-14236.
34. Koebnik, R., and Braun, V. (1993) Insertion derivatives containing segments of up to 16 amino acids identify surface- and periplasm-exposed regions of the FhuA outer membrane receptor of Escherichia coli K-12. J Bacteriol 175: 826-839.
35. Koster, M., van de Vossenberg, J., Leong, J., and Weisbeek, P.J. (1993) Identification and characterization of the pupB gene encoding an inducible ferric-pseudobactin receptor of Pseudomonas putida WCS358. Mol Microbiol 8: 591-601.
36. Koster, M., van Klompenburg, W., Bitter, W., Leong, J., and Weisbeek, P. (1994) Role for the outer membrane ferric siderophore receptor PupB in signal transduction across the bacterial cell envelope. EMBO J 13: 2805-2813.
37. Larsen, R.A., Wood, G.E., and Postle, K. (1993) The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein. Mol Microbiol 10: 943-953.
38. Liu, J., Rutz, J.M., Feix, J.B., and Klebba, P.E. (1993) Permeability properties of a large gated channel within the ferric enterobactin receptor, FepA. Proc Natl Acad Sci USA 90: 10653-10657.
39. Liu, J., Rutz, J.M., Klebba, P.E., and Feix, J.B. (1994) A site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA. Biochemistry 33: 13274-13283.
40. Manavalan, P., and Johnson, Jr, W.C. (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal Biochem 167: 76-85.
41. Moeck, G.S., Fazly Bazzaz, B.S., Gras, M.F., Ravi, T.S., Ratcliffe, M.J.H., and Coulton, J.W. (1994) Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12. J Bacteriol 176: 4250-4259.
42. Moeck, G.S., Ratcliffe, M.J.H., and Coulton, J.W. (1995) Topological analysis of the Escherichia coli ferrichrome-iron receptor by using monoclonal antibodies. J Bacteriol 177: 6118-6125.
43. Murphy, C.K., Kalve, V.I., and Klebba, P.E. (1990) Surface topology of the Escherichia coli K-12 ferric enterobactin receptor. J Bacteriol 172: 2736-2746.
44. Neilands, J.B. (1995) Siderophores: structure and function of microbial iron transport compounds. J Biol Chem 270: 26723-26726.
45. Newton, S.M.C., Klebba, P.E., Michel, V., Hofnung, M, and Charbit, A. (1996) Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model. J Bacteriol 178: 3447-3456.
46. Nikaido, H. (1993) Transport across the bacterial outer membrane. J Bioenergetics Biomemb 6: 581-589.
47. Nikaido, H. (1994) Porins and specific diffusion channels in bacterial outer membranes. J Biol Chem 269: 3905-3908.
48. Nikaido, H., and Saier, Jr, M.H. (1992) Transport proteins in bacteria: common themes in their design. Science 258: 936-942.
49. Nikaido, H., and Vaara, M. (1985) Molecular basis of outer membrane permeability. Microbiol Rev 49: 1-32.
50. Postle, K. (1990) TonB and the Gram-negative dilemma. Mol Microbiol 4: 2019-2025.
51. Postle, K. (1993) TonB protein and energy transduction between membranes. J Bioenergetics Biomemb 6: 591-601.
52. Pressler, U., Staudenmaier, H., Zimmermann, L., and Braun, V. (1988) Genetics of the iron dicitrate transport system of Escherichia coli. J Bacteriol 170: 2716-2724.
53. Rosenbusch, J.P. (1974) Characterization of the major envelope protein from Escherichia coli. J Biol Chem 249: 8019-8029.
54. Rost, B., and Sander, C. (1993) Prediction of protein structure at better than 70% accuracy. J Mol Biol 232: 584-599.
55. Rost, B., and Sander, C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-72.
56. Rost, B., Sander, C., and Schneider, R. (1994) PHD-an automatic mail server for protein secondary structure prediction. CABIOS 10: 53-60.
57. Rutz, J.M., Liu, J., Lyons, J.A., Goranson, J., Armstrong, S.K., McIntosh, M.A., Feix, J.B., and Klebba, P.E. (1992) Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. Science 258: 471-475.
58. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. 2nd edn. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
59. Schirmer, T., Keller, T.A., Wang, Y.F., and Rosenbusch, J.P. (1995) Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267: 512-514.
60. Schöffler, H., and Braun, V. (1989) Transport across the outer membrane of Escherichia coli K-12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol Gen Genet 217: 378-383.
61. Silhavy, T.J., Berman, M.L., and Enquist, L.W. (1984) Experiments with Gene Fusions. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
62. Skare, J.T., Ahmer, B.M.M., Seachord, C.L., Darveau, R.P., and Postle, K. (1993) Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA. J Biol Chem 268: 16302-16308.
63. Srikumar, R., Dahan, D., Gras, M.F., Ratcliffe, M.J.H., van Alohen, L., and Coulton, J.W. (1992) Antigenic sites on porin of Haemophilus influenzae type b: mapping with synthetic peptides and evaluation of structure predictions. J Bacteriol 174: 4007-4016.
64. Susi, H., and Byler, D.M. (1986) Resolution-enhancement Fourier transform infrared spectroscopy of enzymes. Meth Enzymol 130: 290-311.
65. Woody, R.W. (1995) Circular dichroism. Meth Enzymol 246: 34-71.