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Heme acquisition by hemophores

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Abstract

Bacterial hemophores are secreted to the extracellular medium, where they scavenge heme from various hemoproteins due to their higher affinity for this compound, and return it to their specific outer membrane receptor. HasR, the outer membrane receptor of the HasA hemophore, assumes multiple functions which require various energy levels. Binding of heme and, of heme-free or heme-loaded hemophores is energy-independent. Heme transfer from the holo-hemophore to the outer membrane receptor is also energy-independent. In contrast, heme transport and hemophore release require basal or high levels of TonB and proton motive force, respectively. In addition, HasR is a component of a signaling cascade, regulating expression of the has operon via specific sigma and anti-sigma factors encoded by genes clustered at the has operon. The signal is the heme landing on HasR in the presence of the hemophore in its apo form. The has system is the only system thus far characterized in which the anti-sigma factor is submitted to the same signaling cascade as the target operon. Specific autoregulation of the has system, combined with negative regulation by the Fur protein, permits bacterial adaptation to the available iron source. In the presence of a heme-loaded hemophore, inactive anti-sigma factor is accumulated and can be activated as soon as the heme source dries up. Hence, the has system, instead of being submitted to amplification like other systems regulated by sigma anti-sigma factors, functions by pulses triggered by heme availability.

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Authors and Affiliations

  1. Unité des Membranes Bactériennes, Département de Microiologie, URA CNRS 2172 Institut Pasteur, 25, rue du Dr. Roux, 75024, Paris Cedex 15, France

    S. Cescau, H. Cwerman, S. Létoffé, P. Delepelaire, C. Wandersman & F. Biville

Authors
  1. S. Cescau
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  2. H. Cwerman
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  3. S. Létoffé
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  4. P. Delepelaire
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  5. C. Wandersman
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  6. F. Biville
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Correspondence to F. Biville.

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Cescau, S., Cwerman, H., Létoffé, S. et al. Heme acquisition by hemophores. Biometals 20, 603–613 (2007). https://doi.org/10.1007/s10534-006-9050-y

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  • DOI: https://doi.org/10.1007/s10534-006-9050-y

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