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Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli
- Source :
- PLoS ONE, Vol 8, Iss 2, p e56529 (2013), PLoS ONE
- Publication Year :
- 2013
- Publisher :
- Public Library of Science (PLoS), 2013.
-
Abstract
- EfeUOB-like tripartite systems are widespread in bacteria and in many cases they are encoded by genes organized into iron-regulated operons. They consist of: EfeU, a protein similar to the yeast iron permease Ftrp1; EfeO, an extracytoplasmic protein of unknown function and EfeB, also an extracytoplasmic protein with heme peroxidase activity, belonging to the DyP family. Many bacterial EfeUOB systems have been implicated in iron uptake, but a prefential iron source remains undetermined. Nevertheless, in the case of Escherichia coli, the EfeUOB system has been shown to recognize heme and to allow extracytoplasmic heme iron extraction via a deferrochelation reaction. Given the high level of sequence conservations between EfeUOB orthologs, we hypothesized that heme might be the physiological iron substrate for the other orthologous systems. To test this hypothesis, we undertook characterization of the Staphylococcus aureus FepABC system. Results presented here indicate: i) that the S. aureus FepB protein binds both heme and PPIX with high affinity, like EfeB, the E. coli ortholog; ii) that it has low peroxidase activity, comparable to that of EfeB; iii) that both FepA and FepB drive heme iron utilization, and both are required for this activity and iv) that the E. coli FepA ortholog (EfeO) cannot replace FepA in FepB-driven iron release from heme indicating protein specificity in these activities. Our results show that the function in heme iron extraction is conserved in the two orthologous systems.
- Subjects :
- Hemeproteins
Staphylococcus aureus
Operon
Iron
Protoporphyrins
lcsh:Medicine
Receptors, Cell Surface
Heme
Biology
medicine.disease_cause
Biochemistry
Microbiology
chemistry.chemical_compound
Model Organisms
Bacterial Proteins
Microbial Physiology
FepA
medicine
Escherichia coli
lcsh:Science
Integral membrane protein
Microbial Pathogens
Multidisciplinary
Permease
Membrane transport protein
Escherichia coli Proteins
lcsh:R
Membrane Transport Proteins
Proteins
Bacteriology
Bacterial Biochemistry
chemistry
biology.protein
lcsh:Q
Periplasmic Proteins
Carrier Proteins
Peroxidase
Bacterial Outer Membrane Proteins
Protein Binding
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 8
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....b6cdc7878069fe7b197ee19a6c1b7a47