Role of the Twin-Arginine Translocation Pathway in Staphylococcus

被引:66
作者
Biswas, Lalitha [1 ]
Biswas, Raja [1 ]
Nerz, Christiane [1 ]
Ohlsen, Knut [2 ]
Schlag, Martin [1 ]
Schaefer, Tina [2 ]
Lamkemeyer, Tobias [3 ]
Ziebandt, Anne-Kathrin [1 ]
Hantke, Klaus [1 ]
Rosenstein, Ralf [1 ]
Goetz, Friedrich [1 ]
机构
[1] Univ Tubingen, Inst Microbial Genet, D-72076 Tubingen, Germany
[2] Univ Wurzburg, Inst Mol Infect Biol, Wurzburg, Germany
[3] Univ Tubingen, Interfak Inst Zellbiol, Proteome Ctr Tubingen, D-72076 Tubingen, Germany
关键词
BACILLUS-SUBTILIS; LEGIONELLA-PNEUMOPHILA; PROTEIN SECRETION; ESCHERICHIA-COLI; HUMAN SKIN; CELL-WALL; AUREUS; CARNOSUS; EXPORT; HAEMOLYTICUS;
D O I
10.1128/JB.00642-09
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 (Delta tatAC) 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 Delta tatAC and Delta tat-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.
引用
收藏
页码:5921 / 5929
页数:9
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