Details
| Original language | English |
|---|---|
| Pages (from-to) | 2848-2858 |
| Number of pages | 11 |
| Journal | FEBS letters |
| Volume | 591 |
| Issue number | 18 |
| Publication status | Published - Sept 2017 |
Abstract
Translocation of folded proteins by the Tat system of Escherichia coli is believed to rely on the presence of phosphatidylethanolamine (PE) and the negatively charged phospholipids cardiolipin (CL) and phosphatidylglycerol (PG). Here, we show that while PE is indeed essential for activity, the Tat system is fully functional in a clsA/clsB/clsC deletion strain lacking CL, and in a pgsA deletion strain lacking both PG and CL during aerobic growth on complex media. In contrast to early studies that relied on strains with reduced lipid levels, this study therefore demonstrates that PG and CL are dispensable for Tat transport. The lack of these lipids may be compensated by other anionic phospholipids such as phosphatidic acid, CDP-diacylglycerol or N-acyl-PE.
Keywords
- cardiolipin, phosphatidylethanolamine, phosphatidylglycerol, protein translocation, twin-arginine translocation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS letters, Vol. 591, No. 18, 09.2017, p. 2848-2858.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid
AU - Rathmann, Claudia
AU - Schlösser, Amelie S.
AU - Schiller, Jürgen
AU - Bogdanov, Mikhail
AU - Brüser, Thomas
N1 - Funding Information: We thank Ziqiang Guan for donation of strain BKT29, and Kouji Matsumoto for strain GN10/ pMS5, Denise Mehner for construction of strain DM1907, and Sybille Traupe for technical support. We especially thank William Dowhan for support and discussions. MB was supported by National Institutes of Health grant R37 GM 20478 and the John Dunn Research Foundation awarded to William Dowhan, and TB was supported by funding of the State of Lower Saxony. Publisher Copyright: © 2017 Federation of European Biochemical Societies Copyright: Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2017/9
Y1 - 2017/9
N2 - Translocation of folded proteins by the Tat system of Escherichia coli is believed to rely on the presence of phosphatidylethanolamine (PE) and the negatively charged phospholipids cardiolipin (CL) and phosphatidylglycerol (PG). Here, we show that while PE is indeed essential for activity, the Tat system is fully functional in a clsA/clsB/clsC deletion strain lacking CL, and in a pgsA deletion strain lacking both PG and CL during aerobic growth on complex media. In contrast to early studies that relied on strains with reduced lipid levels, this study therefore demonstrates that PG and CL are dispensable for Tat transport. The lack of these lipids may be compensated by other anionic phospholipids such as phosphatidic acid, CDP-diacylglycerol or N-acyl-PE.
AB - Translocation of folded proteins by the Tat system of Escherichia coli is believed to rely on the presence of phosphatidylethanolamine (PE) and the negatively charged phospholipids cardiolipin (CL) and phosphatidylglycerol (PG). Here, we show that while PE is indeed essential for activity, the Tat system is fully functional in a clsA/clsB/clsC deletion strain lacking CL, and in a pgsA deletion strain lacking both PG and CL during aerobic growth on complex media. In contrast to early studies that relied on strains with reduced lipid levels, this study therefore demonstrates that PG and CL are dispensable for Tat transport. The lack of these lipids may be compensated by other anionic phospholipids such as phosphatidic acid, CDP-diacylglycerol or N-acyl-PE.
KW - cardiolipin
KW - phosphatidylethanolamine
KW - phosphatidylglycerol
KW - protein translocation
KW - twin-arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=85029856115&partnerID=8YFLogxK
U2 - 10.1002/1873-3468.12794
DO - 10.1002/1873-3468.12794
M3 - Article
C2 - 28815570
AN - SCOPUS:85029856115
VL - 591
SP - 2848
EP - 2858
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 18
ER -