Downregulation of Tsx and OmpW and upregulation of OmpX are required for iron homeostasis in Escherichia coli

Journal of Proteome Research

Volumn 7, Issue 3, 2008, Pages 1235-1243

  Lin, Xiang Min ^a   Wu, Li Na ^a   Li, Hui ^a,b   Wang, San Ying ^c   Peng, Xuan Xian ^a  

^a SUN YAT SEN UNIVERSITY   (China)

^b GUANGXI UNIVERSITY   (China)

^c XIAMEN UNIVERSITY   (China)

Author keywords

Escherichia coli K 12; Iron limit; Outer membrane proteins; Proteomic

Indexed keywords

IRON; OUTER MEMBRANE PROTEIN; PROTEIN OMPW; PROTEIN OMPX; PROTEIN TSX; SARCOSINE; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; HYDROLASE; OMPW PROTEIN, E COLI; OMPX PROTEIN, E COLI; PRIMER DNA; TSX PROTEIN, E COLI; VIRUS RECEPTOR;

ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; DOWN REGULATION; ESCHERICHIA COLI K 12; GENE DELETION; GENE EXPRESSION; HOMEOSTASIS; NONHUMAN; PRIORITY JOURNAL; UPREGULATION; VALIDATION PROCESS; ESCHERICHIA COLI; METABOLISM; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PROTEOMICS; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ESCHERICHIA COLI; ESCHERICHIA COLI K12;

BACTERIAL OUTER MEMBRANE PROTEINS; BASE SEQUENCE; DNA PRIMERS; DOWN-REGULATION; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HOMEOSTASIS; HYDROLASES; IRON; POLYMERASE CHAIN REACTION; PROTEOMICS; RECEPTORS, VIRUS;

EID: 44449174726     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr7005928     Document Type: Article

References (34)

1. Andrews, S. C; Robinson, A. K.; Rodriguez-Quinones, F. Bacterial iron homeostasis. FEMS Microbiol. Rev. 2003, 27, 215-237.
2. Lin, J.; Huang, S.; Zhang, Q. Outer membrane proteins: Key players for bacterial adaptation in host niches. Microbes Infect. 2002, 4, 325-331.
3. Otto, B. R.; Verweij-van Vught, A. M.; MacLaren, D. M. Transferrins and heme-compounds as iron sources for pathogenic bacteria. Crit. Rev. Microbiol. 1992, 18, 217-233.
4. Faraldo-Gomez, I. D.; Sansom, M. S. Acquisition of siderophores in gram-negative bacteria. Nat. Rev. Mol. Cell Biol. 2003, 4, 105-116.
5. Trias, J.; Nikaido, H. Outer membrane protein d2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 1990, 34, 52-57.
6. Xu, C. X.; Wang, S. Y.; Ren, H. X.; Lin, X. M.; Wu, L. N.; Peng, X. X. Proteomic analysis on the expression of outer membrane proteins of Vibrio alginolyticus at different sodium concentrations. Proteomics 2005, 5, 3142-3152.
7. Peng, X. X.; Xu, C. X.; Ren, H. X.; Lin, X. M.; Wu, L.; Wang, S. Y. Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Pseudomonas aeruginosa responding to ampicilin, kanamycin, and tetracycline resistance. J. Proteome Res. 2005, 4, 2257-2265.
8. Xu, C. X.; Lin, X. M.; Ren, H. X.; Zhang, Y. N.; Wang, S. Y.; Peng, X. X. Analysis of outer membrane proteome of Escherichia coli related to resistance to ampicillin and tetracycline. Proteomics 2006, 6, 462-473.
9. Sato, M.; Machida, K.; Arikado, E.; Saito, H.; Kakegawa, T.; Kobayashi, H. Expression of outer membrane proteins in Escherichia coli growing at acid pH. Appl. Environ. Microbiol. 2000, 66, 943-947.
10. Beddek, A. J.; Sheehan, B. J.; Bosse, J. T.; Rycroft, A. N.; Kroll, J. S.; Langford, P. R. Two TonB systems in Actinobacillus pleuropneumonias Their roles in iron acquisition and virulence. Infect. Immun. 2004, 72, 701-708.
11. Hantke, K.; Nicholson, G.; Rabsch, W.; Winkelmann, G. Salmoch-elins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3677-3682.
12. Molloy, M. P.; Herbert, B. R.; Slade, M. B.; Rabilloud, T.; Nouwens, A. S.; Williams, K. L.; Gooley, A. A. Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 2000, 267, 2871-2881.
13. McHugh, J. P.; Rodriguez-Quinones, F.; Abdul-Tehrani, H.; Svis-tunenko, D. A.; Poole, R. K.; Cooper, C. E.; Andrews, S. C. Global iron-dependent gene regulation in Escherichia coli. A new mechanism for iron homeostasis. J. Biol. Chem. 2003, 278, 29478-29486.
14. Buchanan, S. K.; Smith, B. S.; Venkatramani, L.; Xia, D.; Esser, L.; Palnitkar, M.; Chakraborty, R.; van der Helm, D.; Deisenhofer, J. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat. Struct. Biol. 1999, 6, 56-63.
15. Boulanger, P.; le Maire, M.; Bonhivers, M.; Dubois, S.; Desmadril, M.; Letellier, L. Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Biochemistry 1996, 35, 14216-14224.
16. Locher, K. P.; Rees, B.; Koebnik, R.; Mitschler, A.; Moulinier, L.; Rosenbusch, J. P.; Moras, D. Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and fer-richrome-bound states reveal allosteric changes. Cell 1998, 95, 771-778.
17. Huang, C. Z.; Lin, X. M.; Wu, L. N.; Zhang, D. F.; Liu, D.; Wang, S. Y.; Peng, X. X. Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins. J. Proteome Res. 2006, 5, 3268-3276.
18. Wosten, M. M.; Kox, L. F.; Chamnongpol, S.; Soncini, F. C; Groisman, E. A. A signal transduction system that responds to extracellular iron. Cell 2000, 103, 113-125.
19. Baba, T.; Ara, T.; Hasegawa, M.; Takai, Y.; et al. Construction of Escherichia coliK-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2006, 2, 1-11.
20. Li, H.; Lin, X. M.; Wang, S. Y.; Peng, X. X. Identification and antibody-therapeutic targeting of chloramphenicol-resistant outer membrane proteins in Escherichia coli. J. Proteome Res. 2007, 6, 3628-3636.
21. Peng, X. X.; Wu, Y. J.; Chen, J. G.; Wang, S. Y. Proteomic approach to identify acute phase response-related proteins with low molecular weight in loach skin following injury. Proteomics 2004, 4, 3989-3997.
22. Hantke, K. Iron and metal regulation in bacteria. Curr. Opin. Microbiol. 2001, 4, 172-177.
23. Maier, C.; Bremer, E.; Schmid, A.; Benz, R. Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli demonstration of a nucleoside-specific binding site. J. Biol. Chem. 1988, 263, 2493-2499.
24. Bremer, E.; Middendorf, A.; Martinussen, J.; Valentin-Hansen, P. Analysis of the Tsx gene, which encodes a nucleoside-specific channel-forming protein (Tsx) in the outer membrane of Escherichia coli. Gene 1990, 96, 59-65.
25. Maier, C; Middendorf, A.; Bremer, E. Analysis of a mutated phage t6 receptor protein of Escherichia coli k 12. Mol. Gen. Genet. 1990, 221, 491-494.
26. Hong, H.; Patel, D. R.; Tamm, L. K.; van den, B. B. The outer membrane protein OmpW forms an eight-stranded β-barrel with a hydrophobic channel. J Biol. Chem. 2006, 281, 7568-7577.
27. Albrecht, R.; Zeth, K.; Soding, J.; Lupas, A; Linke, D. Expression, crystallization and preliminary X-ray crystallographic studies of the outer membrane protein OmpW from Escherichia coli. Acta Crystallogr. 2006, F62, 415-418.
28. Pilsl, H.; Smajs, D.; Braun, V. Characterization of colicin s4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane.J. Bacteriol. 1999, 181, 3578-3581.
29. Paustian, M. L.; May, B. J.; Kapur, V. Pasteurella multocida gene expression in response to iron limitation. Infect. Immun. 2001, 69, 4109-4115.
30. Thompson, D. K.; Beliaev, A. S.; Giometti, C. S.; Tollaksen, S. L.; Khare, T.; Lies, D. P.; Nealson, K. H.; Lim, H.; Yates, J., III; Brandt, C. C.; Tiedje, J. M.; Zhou, J. Transcriptional and proteomic analysis of a ferric uptake regulator (fur) mutant of Shewanella oneidensis: Possible involvement of fur in energy metabolism, transcriptional regulation, and oxidative stress. Appl. Environ. Microbiol. 2002, 68, 881-892.
31. Xu, C. X.; Ren, H. X.; Wang, S. Y.; Peng, X. X. Proteomic analysis of salt-sensitive outer membrane proteins of Vibrio parahaemolyticus. Res. Microbiol. 2004, 155, 835-842.
32. Mecsas, J.; Welch, R.; Erickson, J. W.; Gross, C. A. Identification and characterization of an outer membrane protein, ompx, in Escherichia coli that is homologous to a family of outer membrane proteins including AiL of Yersinia enterocolitica. J. Bacteriol. 1995, 177, 799-804.
33. Vogt, J.; Schulz, G. E. The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Struct. Folding Des. 1999, 7, 1301-1309.
34. Stancik, L. M.; Stancik, D. M.; Schmidt, B.; Bamhart, D. M.; Yoncheva, Y. N.; Slonczewski, J. L. pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli. J. Bacteriol. 2002, 184, 4246-4258.