期刊
FEBS LETTERS
卷 581, 期 2, 页码 259-264出版社
WILEY
DOI: 10.1016/j.febslet.2006.12.022
关键词
tat secretion; Rieske Fe/S protein; membrane; insertion; trypsin sensitivity; 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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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