Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins

Henderson, Douglas P.; Payne, Shelley M.

doi:10.1128/jb.176.11.3269-3277.1994

Cited by 120 publications

(131 citation statements)

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“…Analysis of the various V. cholerae TonBdependent outer membrane proteins indicates that there are differences in the TonB boxes, the regions that are thought to interact with TonB. The putative TonB box of V. cholerae IrgA resembles that of E. coli K12 (Goldberg et al, 1992) (Nau and Konisky, 1989), whereas that of HutA is distinctly different (Henderson and Payne, 1994a), and no TonB box has been identified in the vibriobactin receptor ViuA . Therefore, optimal functioning of all the iron-regulated outer membrane proteins in V. cholerae may require multiple TonB proteins.…”

Section: Discussionmentioning

confidence: 99%

Vibrio cholerae iron transport: haem transport genes are linked to one of two sets of tonB, exbB, exbD genes

Occhino

Wyckoff

Henderson

et al. 1998

Molecular Microbiology

161

203

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SummaryVibrio cholerae was found to have two sets of genes encoding TonB, ExbB and ExbD proteins. The first set (tonB1, exbB1, exbD1) was obtained by complementation of a V. cholerae tonB mutant. In the mutant, a plasmid containing these genes permitted transport via the known V. cholerae high-affinity iron transport systems, including uptake of haem, vibriobactin and ferrichrome. When chromosomal mutations in exbB1 or exbD1 were introduced into a wild-type V. cholerae background, no defect in iron transport was noted, indicating the existence of additional genes that can complement the defect in the wild-type background. Another region of the V. cholerae chromosome was cloned that encoded a second functional TonB/Exb system (tonB2, exbB2, exbD2 ). A chromosomal mutation in exbB2 also failed to exhibit a defect in iron transport, but a V. cholerae strain that had chromosomal mutations in both the exbB1 and exbB2 genes displayed a mutant phenotype similar to that of an Escherichia coli tonB mutant. The genes encoding TonB1, ExbB1, ExbD1 were part of an operon that included three haem transport genes (hutBCD ), and all six genes appeared to be expressed from a single Fur-regulated promoter upstream of tonB1. A plasmid containing all six genes permitted utilization of haem by an E. coli strain expressing the V. cholerae haem receptor, HutA. Analysis of the hut genes indicated that hutBCD, which are predicted to encode a periplasmic binding protein (HutB) and cytoplasmic membrane permease (HutC and HutD), were required to reconstitute the V. cholerae haem transport system in E. coli. In V. cholerae, the presence of hutBCD stimulated growth when haemin was the iron source, but these genes were not essential for haemin utilization in V. cholerae.

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Section: Discussionmentioning

confidence: 99%

Vibrio cholerae iron transport: haem transport genes are linked to one of two sets of tonB, exbB, exbD genes

Occhino

Wyckoff

Henderson

et al. 1998

Molecular Microbiology

161

203

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“…Several Gram-negative pathogens have been reported to have multiple heme uptake systems including S. marcescens (33), S. dysenteriae (34), V. cholera (35), Y. pestis (36), and N. meningitidis (37). In a S. marcescens heme auxotroph in vivo studies have shown the hasR and the non-hemophore hemR genes are differentially regulated by heme and iron (38).…”

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Differential Contributions of the Outer Membrane Receptors PhuR and HasR to Heme Acquisition in Pseudomonas aeruginosa

Smith

Wilks

2015

Journal of Biological Chemistry

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Background: Pseudomonas aeruginosa utilizes extracellular heme as a source of iron on infection of the host. Results: Both PhuR and HasR are required for efficient utilization of heme by P. aeruginosa. Conclusion: Non-redundant outer membrane receptors allow for heme acquisition across a range of physiological conditions. Significance: PhuR and HasR have complimentary roles in heme acquisition and utilization.

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“…Outer membrane receptors for hemoproteins have been identified in some pathogens (4,5), suggesting that the selective recognition of heme-containing compounds occurred at the cell surface. However, the involvement of extracellular proteins in heme uptake was not proposed.…”

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confidence: 99%

“…The pellets were suspended in 100 y1 of SDS sample buffer and boiled for 5 min. The affinity gel was pelleted at 3000 x g for 5 (20 mg/ml), or heme (10 mM). Overnight cultures of S. marcescens were grown in LBD to induce HasA secretion.…”

mentioning

confidence: 99%

Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein.

Létoffé

Ghigo

Wandersman

1994

Proc. Natl. Acad. Sci. U.S.A.

185

174

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Several pathogenic bacteria are able to use heme and hemoproteins as iron sources independent of siderophore production by mechanisms involving outer membrane heme-binding proteins and heme transport systems. Here we show that Serratia marcescens has such a property and we identify an extracellular heme-binding protein, HasA (for heme acquisition system), allowing the release of heme from hemoglobin. This protein is secreted by S. marcescens under conditions of iron depletion and is essential for heme acquisition.

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Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins

Cited by 120 publications

References 39 publications

Vibrio cholerae iron transport: haem transport genes are linked to one of two sets of tonB, exbB, exbD genes

Vibrio cholerae iron transport: haem transport genes are linked to one of two sets of tonB, exbB, exbD genes

Differential Contributions of the Outer Membrane Receptors PhuR and HasR to Heme Acquisition in Pseudomonas aeruginosa

Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein.

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