ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12

Research in Microbiology

Volumn 152, Issue 3-4, 2001, Pages 291-301

  Köster, Wolfgang ^a  

^a SWISS FEDERAL INSTITUTE OF AQUATIC SCIENCE AND TECHNOLOGY   (Switzerland)

Author keywords

ABC transporter; Binding proteins; Heme; Iron uptake; Siderophore; Vitamin B12

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; ADHESIN; AEROBACTIN; BINDING PROTEIN; CYANOCOBALAMIN; FERRICHROME; FERRIOXAMINE; GRISEIN; HEME; HYDROXAMIC ACID; IRON; LACTOFERRIN; RHODOTORULIC ACID; SIDEROPHORE; TRANSFERRIN;

ARTICLE; BACTERIAL MEMBRANE; BACTERIAL OUTER MEMBRANE; BACTERIAL VIRULENCE; CRYSTAL STRUCTURE; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; IRON TRANSPORT; MEMBRANE STRUCTURE; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ATP-BINDING CASSETTE TRANSPORTERS; CELL MEMBRANE; CONSERVED SEQUENCE; ESCHERICHIA COLI; FERRIC COMPOUNDS; HEME; INOSINE MONOPHOSPHATE; IRON; PHYLOGENY; SIDEROPHORES; SUBSTRATE SPECIFICITY; VITAMIN B 12;

EID: 0343395846     PISSN: 09232508     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-2508(01)01200-1     Document Type: Article

References (32)

1. Angerer A., Gaisser S., Braun V. Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic binding-protein-dependent iron transport mechanism. J. Bacteriol. 172:1990;572-578.
2. Braun V., Hantke K., Köster W. Bacterial iron transport: mechanisms, genetics, and regulation. Met. Ions Biol. Syst. 35:1998;67-145.
3. Clarke T.E., Ku S.Y., Dougan D.R., Vogel H.J., Tari L.W. The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat. Struct. Biol. 7:2000;287-291.
4. Cornelissen C.N., Sparling P.F. Iron piracy: acquisition of transferrin-bound iron by bacterial pathogens. Mol. Microbiol. 14:1994;843-850.
5. Crosa J.H. Signal transduction and transcriptional and post transcriptional control of iron-regulated genes in bacteria. Microbiol. Mol. Biol. Rev. 61:1997;319-336.
6. Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 9:1985;2287-2293.
7. Expert D., Enard C., Masclaux C. The role of iron in plant host-pathogen interactions. Trends Microbiol. 4:1996;232-237.
8. Genco C.A., Desai P.J. Iron acquisition in the pathogenic Neisseria. Trends Microbiol. 4:1996;179-184.
9. Glass J.I., Lefkovitz E.J., Glass J.S., Helner C.R., Chen E.Y., Cassell G.H. The complete sequence of the mucosal pathogen Ureaplasma urealyticum. Nature. 407:2000;757-762.
10. 12. Microbiology. 144:1998;2759-2769.
11. 12 transport in Escherichia coli: energy coupling between membranes. Mol. Microbiol. 4:1990;2027-2033.
12. Köster W. Transport of iron(III) hydroxamates across the cytoplasmic membrane of Escherichia coli. Trautwein A.X. Bioinorganic Chemistry, Transition Metals in Biology and their Coordination Chemistry. 1997;56-68 Wiley-VCH.
13. Köster W., Böhm B. Point mutations in 2 conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport. Mol. Gen. Genet. 232:1992;399-407.
14. Köster W.L., Actis L.A., Waldbeser L.S., Tolmasky M.E., Crosa J.H. Molecular characterization of the iron transport system mediated by the pJM1-plasmid in Vibrio anguillarum 775. J. Biol. Chem. 266:1991;23829-23833.
15. Lee Y.H., Deka R.K., Norgard M.V., Radolf J.D., Hasemann C.A. Treponema pallidum TroA is a periplasmic zinc binding protein with a helical backbone. Nat. Struct. Biol. 6:1999;628-633.
16. Lawrence M.C., Pilling P.A., Epa V.C., Berry A.M., Ogunniyi A.D., Paton J.C. The crystal structure of pneumococcal surface antigen PsaA reveals a metal binding site and a novel structure for a putative ABC-type binding protein. Structure. 15:1988;1553-1561.
17. Mademidis A., Killmann H., Kraas W., Flechsler I., Jung G., Braun V. ATP-dependent ferric hydroxamate transport system in Escherichia coli: periplasmic FhuD interacts with a periplasmic and with a transmembrane/cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping. Mol. Microbiol. 26:1997;1109-1123.
18. Mietzner T.A., Tencza S.B., Adhikari P., Vaughan K.G., Nowalk A.J. Fe(III) periplasm-to-cytosol transporters of gram-negative pathogens. Curr. Top. Microbiol. Immunol. 225:1998;113-135.
19. Moeck G.S., Coulton J.W. TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport. Mol. Microbiol. 28:1998;675-681.
20. Postle K. Active transport by customized beta-barrels. Nat. Struct. Biol. 6:1999;3-6.
21. Quiocho F.A., Ledvina P.S. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 20:1996;17-25.
22. Rohrbach M.R., Braun V., Köster W. Ferrichrome transport in Escherichia coli K-12: altered substrate specifity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB. J. Bacteriol. 177:1995;7186-7193.
23. Saurin W., Köster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 12:1994;993-1004.
24. Schryvers A.B., Bonnah R., Yu R.H., Wong H., Retzer M. Bacterial lactoferrin receptors. Adv. Exp. Med. Biol. 443:1998;123-133.
25. Schryvers A., Stojilkovic I. Iron acquisition systems in the pathogenic Neisseria. Mol. Microbiol. 32:1999;1117-1123.
26. Schultz-Hauser G., Köster W., Schwarz H., Braun V. Iron (III) hydroxamate transport in Escherichia coli K-12: FhuB-mediated membrane association of the FhuC protein and negative complementation of fhuC mutants. J. Bacteriol. 174:1992;2305-2311.
27. Sprencel C., Cao Z., Qi Z., Scott D.C., Montague M.A., Ivanoff N., Xu J., Raymond K.M., Newton S.M., Klebba P.E. Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB. J. Bacteriol. 182:2000;5359-5364.
28. Stover C.K. Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature. 406:2000;959-964.
29. Vasil M.-L., Ochsner U.A. The response of Pseudomonas aeruginosa to iron: genetics, biochemistry and virulence. Mol. Microbiol. 34:1999;399-413.
30. Vergne A.F., Walz A.J., Miller M.J. Iron chelators from mycobacteria (1954-1999) and potential therapeutic applications. Na. Prod. Rep. 17:2000;99-116.
31. Wandersman C., Stojilkovic I. Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr. Opin. Microbiol. 2000;215-220.
32. Weinberg E.D. The Lactobacillus anomaly: total iron abstinence. Perspect. Biol. Med. 40:1997;578-583.