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A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
Abstract
The utilization by Serratia marcescens of heme bound to hemoglobin requires HasA, an extracellular heme-binding protein. This unique heme acquisition system was studied in an Escherichia coli hemA mutant that was a heme auxotroph. We identified a 92-kDa iron-regulated S. marcescens outer membrane protein, HasR, which alone enabled the E. coli hemA mutant to grow on heme or hemoglobin as a porphyrin source. The concomitant secretion of HasA by the HasR-producing hemA mutant greatly facilitates the acquisition of heme from hemoglobin. This is the first report of a synergy between an outer membrane protein and an extracellular heme-binding protein, HasA, acting as a heme carrier, which we termed a hemophore.
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“HasR can also bind free heme and hemoglobin-bound heme, but these processes are less efficient than HasA-mediated heme acquisition (33, 57).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [33]
In the citing paper
“The HasA system encodes an export complex (HasDEF), a hemophore receptor (HasR), and regulatory proteins (HasI and HasS) (7, 15, 33, 97, 116).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [33]
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Metadata
- Authors
- Ghigo, J. M., Létoffé, S., & Wandersman, C.
- Affiliations
- Unité de Physiologie Cellulaire, Institut Pasteur (CNRS URA 1300), Paris, France.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1997-06
- Volume
- 179
- Issue
- 11
- Pages
- 3572-3579
- ISSN
- 0021-9193
- 1098-5530
- Cited by
- 164
- References
- 1
- Language
- en
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