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The twin‐arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila
Author(s) -
De Buck Emmy,
Vranckx Leen,
Meyen Eef,
Maes Liesbeth,
Vandersmissen Liesbeth,
Anné Jozef,
Lammertyn Elke
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.022
Subject(s) - legionella pneumophila , chromosomal translocation , chemistry , arginine , microbiology and biotechnology , legionella , membrane , twin arginine translocation pathway , biophysics , biochemistry , membrane protein , biology , bacteria , membrane transport protein , genetics , amino acid , gene
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.