title: Role of the twin-arginine translocation pathway in Staphylococcus.
abstract: In Staphylococcus, the twin-arginine translocation (Tat) pathway is present only in some species and is composed of TatA and TatC. The tatAC operon is associated with the fepABC operon, which encodes homologs to an iron-binding lipoprotein, an iron-dependent peroxidase (FepB), and a high-affinity iron permease. The FepB protein has a typical twin-arginine (RR) signal peptide. The tat and fep operons constitute an entity that is not present in all staphylococcal species. Our analysis was focused on Staphylococcus aureus and S. carnosus strains. Tat deletion mutants (DeltatatAC) were unable to export active FepB, indicating that this enzyme is a Tat substrate. When the RR signal sequence from FepB was fused to prolipase and protein A, their export became Tat dependent. Since no other protein with a Tat signal could be detected, the fepABC-tatAC genes comprise not only a genetic but also a functional unit. We demonstrated that FepABC drives iron import, and in a mouse kidney abscess model, the bacterial loads of DeltatatAC and Deltatat-fep mutants were decreased. For the first time, we show that the Tat pathway in S. aureus is functional and serves to translocate the iron-dependent peroxidase FepB.
authors.affiliation: Mikrobielle Genetik, Universität Tübingen, Tübingen, Germany.
authors.forename: Lalitha
authors.initials: L
authors.lastname: Biswas
authors.forename: Raja
authors.initials: R
authors.lastname: Biswas
authors.forename: Christiane
authors.initials: C
authors.lastname: Nerz
authors.forename: Knut
authors.initials: K
authors.lastname: Ohlsen
authors.forename: Martin
authors.initials: M
authors.lastname: Schlag
authors.forename: Tina
authors.initials: T
authors.lastname: Schäfer
authors.forename: Tobias
authors.initials: T
authors.lastname: Lamkemeyer
authors.forename: Anne-Kathrin
authors.initials: AK
authors.lastname: Ziebandt
authors.forename: Klaus
authors.initials: K
authors.lastname: Hantke
authors.forename: Ralf
authors.initials: R
authors.lastname: Rosenstein
authors.forename: Friedrich
authors.initials: F
authors.lastname: Götz
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000737:chemistry*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D004798:Enzymes / Q000235:genetics / Q000378:metabolism; D005260:Female; D026901:Membrane Transport Proteins; D051379:Mice; D008807:Mice, Inbred BALB C; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D010184:Pancreatic Extracts / Q000235:genetics / Q000378:metabolism; D021382:Protein Sorting Signals / Q000235:genetics / Q000502:physiology*; D021381:Protein Transport / Q000235:genetics / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology*; D013203:Staphylococcal Infections / Q000235:genetics / Q000382:microbiology; D013205:Staphylococcal Protein A / Q000235:genetics / Q000378:metabolism; D013210:Staphylococcus / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D013211:Staphylococcus aureus / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004798:Enzymes; D026901:Membrane Transport Proteins; D010184:Pancreatic Extracts; C070436:Prolipase; D021382:Protein Sorting Signals; D013205:Staphylococcal Protein A; D001120:Arginine