The twin-arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila.
The twin-arginine translocation (Tat) pathway translocates folded proteins across the cytoplasmic membrane. Proteins transported through this secretion system typically carry two arginine residues in their signal peptide that is cleaved off during translocation. Recently, we demonstrated the presence of the Tat pathway in Legionella pneumophila Philadelphia-1 and the Rieske Fe/S protein PetA was one of the predicted Tat substrates. Because we observed that the signal peptide of PetA is not processed and that this protein is still membrane associated in the tat mutants, correct membrane insertion was assayed using a trypsin sensitivity assay. We conclude that the Tat pathway is necessary for correct membrane insertion of L. pneumophila PetA.
De Buck
Emmy
E
Laboratory of Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.
Vranckx
Leen
L
Meyen
Eef
E
Maes
Liesbeth
L
Vandersmissen
Liesbeth
L
Anné
Jozef
J
Lammertyn
Elke
E
D001120:Arginine / Q000378:metabolism; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D014450:Electron Transport Complex III / Q000032:analysis / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000032:analysis / Q000378:metabolism*; D016952:Legionella pneumophila / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D021381:Protein Transport
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D026901:Membrane Transport Proteins; C037989:Rieske iron-sulfur protein; D001120:Arginine; D014450:Electron Transport Complex III