New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?

Trends in Biochemical Sciences

Volumn 33, Issue 7, 2008, Pages 330-338

  Schauer, Kristine ^a,b   Rodionov, Dmitry A ^c,d   de Reuse, Hilde ^a  

^a INSTITUT PASTEUR   (France)

^b INSTITUT CURIE   (France)

^c BURNHAM INSTITUTE   (United States)

^d INSTITUTE FOR INFORMATION TRANSMISSION PROBLEMS   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

CYANOCOBALAMIN; PROTEIN TONB;

BACTERIAL GENOME; BACTEROIDES; CAULOBACTER CRESCENTUS; CELL MEMBRANE; ESCHERICHIA COLI; GENE DELETION; GENE LOCUS; GENE MUTATION; GENE TRANSLOCATION; HELICOBACTER PYLORI; NEISSERIA; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN TRANSPORT; PSEUDOMONAS; REVIEW; XANTHOMONAS CAMPESTRIS;

BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; PHYLOGENY; VITAMIN B 12;

NEGIBACTERIA;

EID: 46149094595     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.04.012     Document Type: Review

References (67)

1. Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67 (2003) 593-656
2. Braun V. Energy transfer between biological membranes. ACS Chem. Biol. 1 (2006) 352-354
3. Braun V., and Endriss F. Energy-coupled outer membrane transport proteins and regulatory proteins. Biometals 20 (2007) 219-231
4. Postle K., and Larsen R.A. TonB-dependent energy transduction between outer and cytoplasmic membranes. Biometals 20 (2007) 453-465
5. Carter D.M., et al. Interactions between TonB from Escherichia coli and the periplasmic protein FhuD. J. Biol. Chem. 281 (2006) 35413-35424
6. Chimento D.P., et al. Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins 59 (2005) 240-251
7. Gumbart J., et al. Mechanics of force propagation in TonB-dependent outer membrane transport. Biophys. J. 93 (2007) 496-504
8. Kim M., et al. Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 11975-11980
9. Larsen R.A., et al. In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli. Mol. Microbiol. 49 (2003) 211-218
10. Letain T.E., and Postle K. TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli. Mol. Microbiol. 24 (1997) 271-283
11. Ma L., et al. Evidence of ball-and-chain transport of ferric enterobactin through FepA. J. Biol. Chem. 282 (2007) 397-406
12. Pawelek P.D., et al. Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science 312 (2006) 1399-1402
13. Shultis D.D., et al. Outer membrane active transport: structure of the BtuB:TonB complex. Science 312 (2006) 1396-1399
14. Raymond K.N., et al. Enterobactin: an archetype for microbial iron transport. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 3584-3588
15. Crosa J.H., and Walsh C.T. Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Mol. Biol. Rev. 66 (2002) 223-249
16. Miethke M., and Marahiel M.A. Siderophore-based iron acquisition and pathogen control. Microbiol. Mol. Biol. Rev. 71 (2007) 413-451
17. Wandersman C., and Delepelaire P. Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58 (2004) 611-647
18. Croft M.T., et al. Algae acquire vitamin B12 through a symbiotic relationship with bacteria. Nature 438 (2005) 90-93
19. Braun V. Active transport of siderophore-mimicking antibacterials across the outer membrane. Drug Resist. Updat. 2 (1999) 363-369
20. Cascales E., et al. Colicin biology. Microbiol. Mol. Biol. Rev. 71 (2007) 158-229
21. Killmann H., et al. 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 (1995) 694-698
22. Perkins-Balding D., et al. Iron transport systems in Neisseria meningitidis. Microbiol. Mol. Biol. Rev. 68 (2004) 154-171
23. Wiener M.C. TonB-dependent outer membrane transport: going for Baroque?. Curr. Opin. Struct. Biol. 15 (2005) 394-400
24. Braun V., and Braun M. Active transport of iron and siderophore antibiotics. Curr. Opin. Microbiol. 5 (2002) 194-201
25. Blanvillain S., et al. Plant carbohydrate scavenging through tonb-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS ONE 2 (2007) e224
26. Neugebauer H., et al. ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus. J. Bacteriol. 187 (2005) 8300-8311
27. Schauer K., et al. Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery. Mol. Microbiol. 63 (2007) 1054-1068
28. Contreras M., et al. Characterization of the roles of NikR, a nickel-responsive pleitropic autoregulator of Helicobacter pylori. Mol. Microbiol. 49 (2003) 947-963
29. Davis G.S., et al. Helicobacter pylori HP1512 is a nickel-responsive NikR-regulated outer membrane protein. Infect. Immun. 74 (2006) 6811-6820
30. Ernst F.D., et al. NikR mediates nickel-responsive transcriptional repression of the Helicobacter pylori outer membrane proteins FecA3 (HP1400) and FrpB4 (HP1512). Infect. Immun. 74 (2006) 6821-6828
31. Gelfand M.S., and Rodionov D.A. Comparative genomics and functional annotation of bacterial transporters. Phys. Life Rev. 5 (2007) 22-49
32. 12 in Escherichia coli. J. Bacteriol. 106 (1971) 745-750
33. Payne M.A., et al. Biphasic binding kinetics between FepA and its ligands. J. Biol. Chem. 272 (1997) 21950-21955
34. Locher K.P., and Rosenbusch J.P. Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes. Eur. J. Biochem. 247 (1997) 770-775
35. Newton S.M., et al. Effect of loop deletions on the binding and transport of ferric enterobactin by FepA. Mol. Microbiol. 32 (1999) 1153-1165
36. Devanathan S., and Postle K. Studies on colicin B translocation: FepA is gated by TonB. Mol. Microbiol. 65 (2007) 441-453
37. Rabsch W., et al. FepA- and TonB-dependent bacteriophage H8: receptor binding and genomic sequence. J. Bacteriol. 189 (2007) 5658-5674
38. Saier Jr. M.H. A functional-phylogenetic system for the classification of transport proteins. J. Cell. Biochem. Suppl. 32-33 (1999) 84-94
39. Mobley H.L., et al. Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditions. Mol. Microbiol. 16 (1995) 97-109
40. Osterman A., and Overbeek R. Missing genes in metabolic pathways: a comparative genomics approach. Curr. Opin. Chem. Biol. 7 (2003) 238-251
41. Overbeek R., et al. Annotation of bacterial and archaeal genomes: improving accuracy and consistency. Chem. Rev. 107 (2007) 3431-3447
42. Gelfand M.S., and Laikova O.N. Prolegomena to the evolution of transcriptional regulation in bacterial genomes. In: Galperin M.Y., and Koonin E.V. (Eds). Frontiers in Computational Genomics (2003), Caister Academic Press 195-216
43. Rodionov D.A. Comparative genomic reconstruction of transcriptional regulatory networks in bacteria. Chem. Rev. 107 (2007) 3467-3497
44. Rodionov D.A., et al. Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters. J. Bacteriol. 188 (2006) 317-327
45. Yang C., et al. Comparative genomics and experimental characterization of N-acetylglucosamine utilization pathway of Shewanella oneidensis. J. Biol. Chem. 281 (2006) 29872-29885
46. Koebnik R. TonB-dependent trans-envelope signalling: the exception or the rule?. Trends Microbiol. 13 (2005) 343-347
47. Rodionov D.A., et al. Comparative genomics of thiamin biosynthesis in prokaryotes. New genes and regulatory mechanisms. J. Biol. Chem. 277 (2002) 48949-48959
48. Ren Q., and Paulsen I.T. Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes. PLoS Comput Biol 1 (2005) e27
49. Xu J., et al. A genomic view of the human-Bacteroides thetaiotaomicron symbiosis. Science 299 (2003) 2074-2076
50. Lee H.S., et al. Molecular characterization of nosA, a Pseudomonas stutzeri gene encoding an outer membrane protein required to make copper-containing N2O reductase. J. Bacteriol. 173 (1991) 5406-5413
51. Mokhele K., et al. A Pseudomonas stutzeri outer membrane protein inserts copper into N2O reductase. J. Bacteriol. 169 (1987) 5721-5726
52. Wunsch P., et al. Requirements for Cu(A) and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida. J. Bacteriol. 185 (2003) 887-896
53. Yoneyama H., and Nakae T. Protein C (OprC) of the outer membrane of Pseudomonas aeruginosa is a copper-regulated channel protein. Microbiology 142 (1996) 2137-2144
54. Lee H.S., et al. Properties of a Pseudomonas stutzeri outer membrane channel-forming protein (NosA) required for production of copper-containing N2O reductase. J. Bacteriol. 171 (1989) 2096-2100
55. Turner P.C., et al. Neisserial TonB-dependent outer-membrane proteins: detection, regulation and distribution of three putative candidates identified from the genome sequences. Microbiology 147 (2001) 1277-1290
56. Reeves A.R., et al. A Bacteroides thetaiotaomicron outer membrane protein that is essential for utilization of maltooligosaccharides and starch. J. Bacteriol. 178 (1996) 823-830
57. Hottes A.K., et al. Transcriptional profiling of Caulobacter crescentus during growth on complex and minimal media. J. Bacteriol. 186 (2004) 1448-1461
58. Tralau T., et al. Transcriptomic analysis of the sulfate starvation response of Pseudomonas aeruginosa. J. Bacteriol. 189 (2007) 6743-6750
59. Felsenstein J. Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods. Methods Enzymol. 266 (1996) 418-427
60. Krewulak K.D., and Vogel H.J. Structural biology of bacterial iron uptake. Biochim. Biophys. Acta (2007) 10.1016/j.bbamem.2007.07.026
61. Higgs P.I., et al. Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB. ExbD and FepA. Mol. Microbiol. 44 (2002) 271-281
62. Hvorup R.N., et al. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317 (2007) 1387-1390
63. Hollenstein K., et al. Structure of an ABC transporter in complex with its binding protein. Nature 446 (2007) 213-216
64. Linton K.J. Structure and function of ABC transporters. Physiology (Bethesda) 22 (2007) 122-130
65. Cescau S., et al. Heme acquisition by hemophores. Biometals 20 (2007) 603-613
66. Letoffe S., et al. Haemophore-mediated bacterial haem transport: evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor. Mol. Microbiol. 41 (2001) 439-450
67. Rodionov D.A., et al. Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes. J. Biol. Chem. 278 (2003) 41148-41159