The twin-arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila

被引：33

作者：

De Buck, Emmy ^{[1
]}

Vranckx, Leen ^{[1
]}

Meyen, Eef ^{[1
]}

Maes, Liesbeth ^{[1
]}

Vandersmissen, Liesbeth ^{[1
]}

Anne, Jozef ^{[1
]}

Lannnertyn, Elke ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Rega Inst Med Res, Bacteriol Lab, B-3000 Louvain, Belgium

来源：

FEBS LETTERS | 2007年 / 581卷 / 02期

关键词：

tat secretion; Rieske Fe/S protein; membrane; insertion; trypsin sensitivity; Legionella pneumophila;

D O I：

10.1016/j.febslet.2006.12.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：259 / 264

页数：6

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