Identification and Characterization of Two Contiguous Operons Required for Aerobactin Transport and Biosynthesis in <i>Vibrio mimicus</i>

Moon, Yong-Hwa; Tanabe, T.; Funahashi, Tatsuya; Shiuchi, Keiichi; Nakao, Hiroshi; Yamamoto, Satoshi

doi:10.1111/j.1348-0421.2004.tb03528.x

Cited by 27 publications

(18 citation statements)

References 44 publications

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“…ato1 encodes a putative acyltransferase with homology to an acyltransferase from A. oryzae (Accession No. BAC78653) and to N 6 ‐hydroxylysine acetyltransferases from bacteria producing the hydroxamate siderophore aerobactin [35]. Moreover, ato1 is placed between fso1 and omo1 , strongly suggesting a direct involvement in ferrichrome A synthesis.…”

Section: Discussionmentioning

confidence: 97%

Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomyceteOmphalotus olearius

Welzel

Eisfeld

Antelo

et al. 2005

FEMS Microbiology Letters

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Under iron deprivation Omphalotus olearius was found to produce the hydroxamate siderophore ferrichrome A. A gene cluster consisting of three genes: fso1, a nonribosomal peptide synthetase whose expression is enhanced in the absence of iron; omo1, a l-ornithine-N(5)-monooxygenase; and ato1, an acyltransferase probably involved in the transfer of the methylglutaconyl residue to N(5)-hydroxyorinithine was identified. The fso1 sequence is interrupted by 48 introns and its derived protein sequence has a similar structure to the homologous genes of Ustilago maydis and Aspergillus nidulans. This is the first report of a nonribosomal peptide synthetase gene and a biosynthetic gene cluster in homobasidiomycetes.

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Section: Discussionmentioning

confidence: 97%

Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomyceteOmphalotus olearius

Welzel

Eisfeld

Antelo

et al. 2005

FEMS Microbiology Letters

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“…Aerobactin, a hydroxamate siderophore found in many enteric bacteria, including E. coli, Shigella, and Salmonella, is also produced by some Vibrio species. Vibrio mimicus (77), Vibrio hollisae (78), and a planktonic marine Vibrio sp. (79) all produce this siderophore.…”

Section: Transport Of Iron Complexesmentioning

confidence: 99%

Vibrio Iron Transport: Evolutionary Adaptation to Life in Multiple Environments

Payne

Mey

Wyckoff

2016

Microbiol Mol Biol Rev

102

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SUMMARYIron is an essential element forVibriospp., but the acquisition of iron is complicated by its tendency to form insoluble ferric complexes in nature and its association with high-affinity iron-binding proteins in the host. Vibrios occupy a variety of different niches, and each of these niches presents particular challenges for acquiring sufficient iron.Vibriospecies have evolved a wide array of iron transport systems that allow the bacteria to compete for this essential element in each of its habitats. These systems include the secretion and uptake of high-affinity iron-binding compounds (siderophores) as well as transport systems for iron bound to host complexes. Transporters for ferric and ferrous iron not complexed to siderophores are also common toVibriospecies. Some of the genes encoding these systems show evidence of horizontal transmission, and the ability to acquire and incorporate additional iron transport systems may have allowedVibriospecies to more rapidly adapt to new environmental niches. While too little iron prevents growth of the bacteria, too much can be lethal. The appropriate balance is maintained in vibrios through complex regulatory networks involving transcriptional repressors and activators and small RNAs (sRNAs) that act posttranscriptionally. Examination of the number and variety of iron transport systems found inVibriospp. offers insights into how this group of bacteria has adapted to such a wide range of habitats.

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“…It is, therefore, worth noting that, in contrast to V. parahaemolyticus, other Vibrio species such as V. mimicus, 32) V. hollisae 33) and V. vulnificus, 34) all of which are capable of utilizing aerobactin, possess respective own ABC transporter genes specific to ferric aerobactin in proximity to their receptor genes. This at least suggests that the ferric aerobactin receptor gene in V. parahaemolyticus might be acquired independently of its transporter genes by horizontal gene transfer.…”

Section: )mentioning

confidence: 99%

Identification and Characterization of Genes Required for Utilization of Desferri-Ferrichrome and Aerobactin in Vibrio parahaemolyticus

Funahashi

Tanabe

Shiuchi

et al. 2009

Biological & Pharmaceutical Bulletin

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In response to iron starvation, many bacteria produce siderophores which mediate high-affinity iron transport enabling iron to be scavenged from their surroundings. [1][2][3] In addition to their native siderophores, some bacteria are endowed with the uptake systems for heterologous siderophores produced by other bacterial and fungal species. In gram-negative bacteria, these siderophores loaded with ferric ion are transported via an energy dependent system across the membrane into the cytoplasm. The components of such systems include a receptor protein located in the outer membrane, a periplasmic binding protein and an ATP-binding cassette (ABC) type transporter located in the inner membrane. 2,4)The energy required for transport via the outer membrane receptor is provided by interaction of the receptor with the TonB-ExbB-ExbD complex located in the inner membrane, which couples the proton motive force created by the inner membrane for energy transduction. In general, siderophores display higher receptor specificity than proteins constituting the ABC transport systems. 4) Furthermore, expression of genes responsible for siderophore biosynthesis and uptake of its ferric complex are controlled by concentration of iron in the environment through a global iron-binding repressor called ferric utilization regulation (Fur) protein, with increased expression occurring under iron-limiting conditions. 2,5)Vibrio parahaemolyticus is a gram-negative halophilic bacterium that is found in estuarine waters worldwide and is recognized as a leading cause of food-borne gastroenteritis. 6)V. parahaemolyticus secretes the siderophore vibrioferrin in response to iron starvation.7) The pvsABCDE genes are involved in production 8) and secretion 9) of vibrioferrin, and uptake of its ferric complex occurs via the outer membrane receptor PvuA 10) and the ABC transporter PvuBCDE. have been annotated in the genomic sequences of V. parahaemolyticus RIMD2210633, 15) but none of these genes have been experimentally characterized to date. We report here that the V. parahaemolyticus fhuACDB orthologs are responsible for ferrichrome utilization and that the fhuCDB genes are also needed for transport of ferric aerobactin across the inner membrane. MATERIALS AND METHODSStrains, Plasmids, and Media Bacterial strains and plasmids used in this study are listed in Table 1. Unless otherwise noted, bacterial cells were routinely grown with shaking at 37°C in Luria-Bertani (LB) broth (pH 7.5, 1% tryptone peptone, 0.5% yeast extract) or grown on LB agar plates (1.5% agar) containing 3% (V. parahaemolyticus) and 0.5% (E. coli) NaCl. (LB) media with and without addition of the iron chelator ethylenediamine-di(o-hydroxyphenylacetic acid) (EDDA) (Sigma) at 25 mM were used for growth under ironlimiting (ϪFe) and iron-replete (ϩFe) conditions, respectively. The media for E. coli were supplemented with ampicillin (50 mg/ml) or chloramphenicol (10 mg/ml), when required.Growth Assay V. parahaemolyticus TNB6 which carries a deletion in pvsA of strain AQ3354, result...

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Identification and Characterization of Two Contiguous Operons Required for Aerobactin Transport and Biosynthesis in Vibrio mimicus

Cited by 27 publications

References 44 publications

Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomyceteOmphalotus olearius

Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomyceteOmphalotus olearius

Vibrio Iron Transport: Evolutionary Adaptation to Life in Multiple Environments

Identification and Characterization of Genes Required for Utilization of Desferri-Ferrichrome and Aerobactin in Vibrio parahaemolyticus

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