Identification and characterization of Aeromonas hydrophila genes encoding the outer membrane receptor of ferrioxamine B and an AraC-type transcriptional regulator

References

• Ratledge C, Dover LG. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 2000;54:881–941.10.1146/annurev.micro.54.1.881
   PubMed Web of Science ®Google Scholar
• Miethke M, Marahiel MA. Siderophore-based iron acquisition and pathogen control. Microbiol. Mol. Biol. Rev. 2007;71:413–451.10.1128/MMBR.00012-07
   PubMed Web of Science ®Google Scholar
• Krewulak KD, Vogel HJ. Structural biology of bacterial iron uptake. Biochim. Biophys. Acta. 2008;1778:1781–1804.10.1016/j.bbamem.2007.07.026
   PubMed Web of Science ®Google Scholar
• Escolar L, Pérez-Martin J, de Lorenzo V. Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 1991;181:6223–6229.
   Google Scholar
• Carpenter BM, Whitmire JM, Merrell DS. This is not your mother’s repressor: the complex role of Fur in pathogenesis. Infect. Immun. 2009;77:2590–2601.10.1128/IAI.00116-09
   PubMed Web of Science ®Google Scholar
• Heinrichs DE, Poole K. Cloning and sequence analysis of a gene (pchR) encoding an AraC family activator of pyochelin and ferripyochelin receptor synthesis in Pseudomonas aeruginosa. J. Bacteriol. 1993;175:5882–5889.
   PubMed Web of Science ®Google Scholar
• Fetherston JD, Bearden SW, Perry RD. YbtA, an AraC-type regulator of the Yersinia pestis pesticin/yersiniabactin receptor. Mol. Microbiol. 1996;22:315–325.10.1046/j.1365-2958.1996.00118.x
   PubMed Web of Science ®Google Scholar
• Beaumont FC, Kang HY, Brickman TJ, Armstrong SK. Identification and characterization of alcR, a gene encoding an AraC-like regulator of alcaligin siderophore biosynthesis and transport in Bordetella pertussis and Bordetella bronchiseptica. J. Bacteriol. 1998;180:862–870.
   PubMed Web of Science ®Google Scholar
• Pradel E, Guiso N, Locht C. Identification of AlcR, an AraC-type regulator of alcaligin siderophore synthesis in Bordetella bronchiseptica and Bordetella pertussis. J. Bacteriol. 1998;180:871–880.
   PubMed Web of Science ®Google Scholar
• Tanabe T, Takata N, Naka A, Moon Y-H, Nakao H, Inoue Y, Narimatsu S, Yamamoto S. Identification of an AraC-like regulator gene required for induction of the 78 kDa ferrioxamine B receptor in Vibrio vulnificus. FEMS Microbiol. Lett. 2005;249:309–314.10.1016/j.femsle.2005.06.025
   PubMed Web of Science ®Google Scholar
• Tanabe T, Funahashi T, Miyamoto K, Tsujibo H, Yamamoto S. Identification of genes, desR and desA, required for utilization of desferrioxamine B as a xenosiderophore in Vibrio furnissii. Biol. Pharm. Bull. 2011;34:570–574.10.1248/bpb.34.570
   PubMed Web of Science ®Google Scholar
• Semel JD, Trenholme G. Aeromonas hydrophila water-associated traumatic wound infections: a review. J. Trauma Injury Infect. Crit. Care. 1990;30:324–327.10.1097/00005373-199003000-00011
   PubMed Web of Science ®Google Scholar
• Janda JM, Abbott SL. The genus Aeromonas: taxonomy, pathogenicity, and infection. Clin. Microbiol. Rev. 2010;23:35–73.10.1128/CMR.00039-09
   PubMed Web of Science ®Google Scholar
• Barghouthi S, Young R, Olson MO, Arceneaux JE, Clem LW, Byers BR. Amonabactin, a novel tryptophan- or phenylalanine-containing phenolate siderophore in Aeromonas hydrophila. J. Bacteriol. 1989;171:1811–1816.
   PubMed Web of Science ®Google Scholar
• Telford JR, Raymond KN. Amonabactin: a family of novel siderophores from a pathogenic bacterium. J. Biol. Inorg. Chem. 1997;2:750–761.10.1007/s007750050191
   Web of Science ®Google Scholar
• Funahashi T, Tanabe T, Miyamoto K, Tsujibo H, Maki J, Yamamoto S. Biosci. Biotechnol. Biochem. 2013;77:353–360.
   PubMed Web of Science ®Google Scholar
• Sambrook J, Fritsch EF, Maniatis T. Molecular cloning, a laboratory manual. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1989.
   Google Scholar
• Seshadri R, Joseph SW, Chopra AK, Sha J, Shaw J, Graf J, Haft D, Wu M, Ren Q, Rosovitz MJ, Madupu R, Tallon L, Kim M, Jin S, Vuong H, Stine OC, Ali A, Horneman AJ, Heidelberg JF. Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades. J. Bacteriol. 2006;188:8272–8282.10.1128/JB.00621-06
   PubMed Web of Science ®Google Scholar
• Yamamoto S, Akiyama T, Okujo N, Matsu-ura S, Shinoda S. Demonstration of a ferric vibrioferrin-binding protein in the outer membrane of Vibrio parahaemolyticus. Microbiol. Immunol. 1995;39:759–766.10.1111/mim.1995.39.issue-10
   PubMed Web of Science ®Google Scholar
• Stojiljkovic I, Bäumler AJ, Hantke K. Fur regulon in Gram-negative bacteria. J. Mol. Biol. 1994;236:531–545.10.1006/jmbi.1994.1163
   PubMed Web of Science ®Google Scholar
• Kuroda T, Mizushima T, Tsuchiya T. Physiological roles of three Na+/H+ antiporters in the halophilic bacterium Vibrio parahaemolyticus. Microbiol. Immunol. 2005;49:711–719.10.1111/mim.2005.49.issue-8
   PubMed Web of Science ®Google Scholar
• Heckman KL, Pease LR. Gene splicing and mutagenesis by PCR-driven overlap extension. Nat. Protoc. 2007;2:924–932.10.1038/nprot.2007.132
   PubMed Web of Science ®Google Scholar
• Tanabe T, Funahashi T, Okajima N, Nakao H, Takeuchi Y, Miyamoto K, Tsujibo H, Yamamoto S. The Vibrio parahaemolyticus pvuA1 gene (formerly termed psuA) encodes a second ferric vibrioferrin receptor that requires tonB2. FEMS Microbiol. Lett. 2011;324:73–79.10.1111/fml.2011.324.issue-1
   PubMed Web of Science ®Google Scholar
• Demarre G, Guérout AM, Matsumoto-Mashimo C, Rowe-Magnus DA, Marlière P, Mazel D. A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPα) conjugative machineries and their cognate Escherichia coli host strains. Res. Microbiol. 2005;156:245–255.10.1016/j.resmic.2004.09.007
   PubMed Web of Science ®Google Scholar
• Keen NT, Tamaki S, Kobayashi D, Trollinger D. Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria. Gene. 1988;70:191–197.10.1016/0378-1119(88)90117-5
   PubMed Web of Science ®Google Scholar
• Parales RE, Harwood CS. Construction and use of a new broad-host-range lacZ transcriptional fusion vector, pHRP309, for Gram− bacteria. Gene. 1993;133:23–30.10.1016/0378-1119(93)90220-W
   PubMed Web of Science ®Google Scholar
• Miller JH. Experiments in molecular genetics. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1972. p. 352–355.
   Google Scholar
• Matzanke BF, Anemüller S, Schünemann V, Trautwein AX, Hantke K. FhuF, part of a siderophore-reductase system. Biochemistry. 2004;43:1386–1392.10.1021/bi0357661
   PubMed Web of Science ®Google Scholar
• Lux TM, Lee R, Love J. Complete genome sequence of a free-living Vibrio furnissii sp. nov. strain (NCTC 11218). J. Bacteriol. 2011;193:1487–1488.10.1128/JB.01512-10
   PubMed Web of Science ®Google Scholar
• de Lorenzo V, Wee S, Herrero M, Neilands JB. Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J. Bacteriol. 1987;169:2624–2630.
   PubMed Web of Science ®Google Scholar
• Postle K, Larsen RA. TonB-dependent energy transduction between outer and cytoplasmic membranes. Biometals. 2007;20:453–465.10.1007/s10534-006-9071-6
   PubMed Web of Science ®Google Scholar
• Sean Peacock R, Weljie AM, Peter Howard S, Price FD, Vogel HJ. The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. J. Mol. Biol. 2005;345:1185–1197.10.1016/j.jmb.2004.11.026
   PubMed Web of Science ®Google Scholar
• Steuyvé M, Moons M, Tommassen J. Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J. Mol. Biol. 1991;218:141–148.
   PubMed Web of Science ®Google Scholar
• Gallegos MT, Schleif R, Bairoch A, Hofmann K, Ramos JL. AraC/XylS family of transcriptional regulators. Microbiol. Mol. Biol. Rev. 1997;61:393–410.
   PubMed Web of Science ®Google Scholar
• Balado M, Osorio CR, Lemos ML. Biosynthetic and regulatory elements involved in the production of the siderophore vanchrobactin in Vibrio anguillarum. Microbiology. 2008;154:1400–1413.10.1099/mic.0.2008/016618-0
   PubMed Web of Science ®Google Scholar
• Kwon HJ, Bennik MHJ, Demple B, Ellenberger T. Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA. Nat. Struct. Biol. 2000;7:424–430.
   PubMedGoogle Scholar
• Muller K, Matzanke BF, Schunemann V, Trautwein AX, Hantke K. FhuF, an iron-regulated protein of Escherichia coli with a new type of [2Fe–2S] center. Eur. J. Biochem. 1998;258:1001–1008.10.1046/j.1432-1327.1998.2581001.x
   PubMedGoogle Scholar
• Tortell PD, Maldonado MT, Granger J, Price NM. Marine bacteria and biogeochemical cycling of iron in the oceans. FEMS Microbiol. Ecol. 1999;29:1–11.10.1111/fem.1999.29.issue-1
   Web of Science ®Google Scholar
• Winkelmann G. Ecology of siderophores. In: Crosa JH, Mey AR, Payne SM, editors. Iron transport in bacteria. Washington (DC): ASM Press; 2004. p. 437–450.
   Google Scholar
• Essén SA, Bylund D, Holmström SJ, Moberg M, Lundström US. Quantification of hydroxamate siderophores in soil solutions of podzolic soil profiles in Sweden. BioMetals. 2006;19:269–282.10.1007/s10534-005-8418-8
   PubMed Web of Science ®Google Scholar
• Mawji E, Gledhill M, Milton JA, Tarran GA, Ussher S, Thompson A, Wolff GA, Worsfold PJ, Achterberg EP. Hydroxamate siderophores: occurrence and importance in the Atlantic Ocean. Environ. Sci. Technol. 2008;42:8675–8680.10.1021/es801884r
   PubMed Web of Science ®Google Scholar
• Gledhill M, Buck KN. The organic complexation of iron in the marine environment. Front. Microbiol. 2012;3:1–17.
   PubMed Web of Science ®Google Scholar