Title: The twin-arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila
Authors: De Buck, Emmy ×
Vranckx, Leen
Meyen, Eva
Maes, Liesbeth
Vandersmissen, Liesbeth
Anné, Jozef
Lammertyn, Elke #
Issue Date: Jan-2007
Publisher: Elsevier on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Letters vol:581 issue:2 pages:259-64
Abstract: 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.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Bacteriology (Rega Institute)
Laboratory of Virology and Chemotherapy (Rega Institute)
Academic Center for General Practice
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science