Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 25281-25289 |
| Seitenumfang | 9 |
| Fachzeitschrift | Journal of Biological Chemistry |
| Jahrgang | 283 |
| Ausgabenummer | 37 |
| Publikationsstatus | Veröffentlicht - 12 Sept. 2008 |
| Extern publiziert | Ja |
Abstract
The twin-arginine translocation (Tat) system of bacteria and plant plastids serves to translocate folded proteins across energized biological membranes. In Escherichia coli, the three components TatA, TatB, and TatC mediate this membrane passage. Here we demonstrate that TatA can assemble to form clusters of tube-like structures in vivo. While the presence of TatC is essential for their formation, TatB is not required. The TatA tubes have uniform outer and inner diameters of about 11.5 nm and 6.7 nm, respectively. They align to form a crystalline-like structure in which each tube is surrounded by six TatA tubes. The tube structures become easily detectable even at only a 15-fold overexpression of the tatABC genes. The TatA tubes could also be visualized by fluorescence when untagged TatA was mixed with low amounts of TatA-GFP. The structures were often found in contact with the cell poles. Because TatC is most likely polar in E. coli, as demonstrated by a RR-dependent targeting of translocation-incompatible Tat substrates to the cell poles, and because TatC is required for the formation of aligned TatA tubes, it is proposed that the TatA tubes are initiated at polarly localized TatC.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Journal of Biological Chemistry, Jahrgang 283, Nr. 37, 12.09.2008, S. 25281-25289.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Recombinant expression of tatABC and tatAC results in the formation of interacting cytoplasmic TatA tubes in Escherichia coli
AU - Berthelmann, Felix
AU - Mehner, Denise
AU - Richter, Silke
AU - Lindenstrauss, Ute
AU - Lünsdorf, Heinrich
AU - Hause, Gerd
AU - Brüser, Thomas
N1 - Copyright: Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2008/9/12
Y1 - 2008/9/12
N2 - The twin-arginine translocation (Tat) system of bacteria and plant plastids serves to translocate folded proteins across energized biological membranes. In Escherichia coli, the three components TatA, TatB, and TatC mediate this membrane passage. Here we demonstrate that TatA can assemble to form clusters of tube-like structures in vivo. While the presence of TatC is essential for their formation, TatB is not required. The TatA tubes have uniform outer and inner diameters of about 11.5 nm and 6.7 nm, respectively. They align to form a crystalline-like structure in which each tube is surrounded by six TatA tubes. The tube structures become easily detectable even at only a 15-fold overexpression of the tatABC genes. The TatA tubes could also be visualized by fluorescence when untagged TatA was mixed with low amounts of TatA-GFP. The structures were often found in contact with the cell poles. Because TatC is most likely polar in E. coli, as demonstrated by a RR-dependent targeting of translocation-incompatible Tat substrates to the cell poles, and because TatC is required for the formation of aligned TatA tubes, it is proposed that the TatA tubes are initiated at polarly localized TatC.
AB - The twin-arginine translocation (Tat) system of bacteria and plant plastids serves to translocate folded proteins across energized biological membranes. In Escherichia coli, the three components TatA, TatB, and TatC mediate this membrane passage. Here we demonstrate that TatA can assemble to form clusters of tube-like structures in vivo. While the presence of TatC is essential for their formation, TatB is not required. The TatA tubes have uniform outer and inner diameters of about 11.5 nm and 6.7 nm, respectively. They align to form a crystalline-like structure in which each tube is surrounded by six TatA tubes. The tube structures become easily detectable even at only a 15-fold overexpression of the tatABC genes. The TatA tubes could also be visualized by fluorescence when untagged TatA was mixed with low amounts of TatA-GFP. The structures were often found in contact with the cell poles. Because TatC is most likely polar in E. coli, as demonstrated by a RR-dependent targeting of translocation-incompatible Tat substrates to the cell poles, and because TatC is required for the formation of aligned TatA tubes, it is proposed that the TatA tubes are initiated at polarly localized TatC.
UR - http://www.scopus.com/inward/record.url?scp=54449092519&partnerID=8YFLogxK
U2 - 10.1074/jbc.M707757200
DO - 10.1074/jbc.M707757200
M3 - Article
C2 - 18644791
AN - SCOPUS:54449092519
VL - 283
SP - 25281
EP - 25289
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 37
ER -