Molecular Microbiology · 1998 · 159 citations · 25 references
Life SciencesMicrobiologyMolecular BiologyBacteriologyHost-pathogen InteractionsMedical MicrobiologyBacterial Secretion SystemsHemoglobin PhysiologyIron TransportMembrane ReceptorsAbc Transporter InvolvementBacterial Iron RegulationBacterial Surface ReceptorsEscherichia ColiHeme Iron AcquisitionOuter Membrane Protein SecretionOuter Membrane ProteinsOuter Membrane Structure
The major mechanism by which bacteria acquire free or haemoglobin-bound haem involves direct binding to specific outer membrane receptors. Serratia marcescens also secretes a haem-binding protein, HasA, which functions as a haemophore that catches haem and shuttles it to a cell surface specific outer membrane receptor, HasR. We report the isolation and characterization of hasAp, a gene from Pseudomonas aeruginosa. HasAp is an iron-regulated extracellular haem-binding protein that shares about 50% identity with HasA. HasAp is required for P. aeruginosa utilization of haemoglobin iron. It can replace HasA for HasR-dependent haemoblobin acquisition in a system reconstituted in Escherichia coli. HasAp, like HasA, lacks a signal peptide and is secreted by an ABC transporter. These findings show that haemophore-dependent haem acquisition is not unique to S. marcescens.
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Jon T. Skare, Brian M. M. Ahmer, Carrie L. Seachord et al. · Journal of Biological Chemistry · 1993 · 219 citations · Full text