Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 3644-3648 |
| Seitenumfang | 5 |
| Fachzeitschrift | FEBS letters |
| Jahrgang | 584 |
| Ausgabenummer | 16 |
| Publikationsstatus | Veröffentlicht - Aug. 2010 |
Abstract
The twin-arginine translocation (Tat) system translocates folded proteins across biological membranes. It has been suggested that the Tat system of Escherichia coli can direct Tat substrates to degradation if they are not properly folded [Matos, C.F., Robinson, C. and Di Cola, A. (2008) The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J. 27, 2055-2063; Matos, C.F., Di Cola, A. and Robinson, C. (2009) TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli. EMBO Rep. 10, 474-479]. Contrary to the earlier reports, it is now concluded that reported differences between tested strains were due to variations in expression levels and inclusion body formation. Using the native Tat substrate NrfC and a malfolded variant thereof, we show that the turnover of these proteins is not affected by the absence of all known Tat components. Malfolded NrfC is degraded more quickly than the native protein, indicating that Tat-independent protease systems can recognize malfolded Tat substrates.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biophysik
- Biochemie, Genetik und Molekularbiologie (insg.)
- Strukturelle Biologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: FEBS letters, Jahrgang 584, Nr. 16, 08.2010, S. 3644-3648.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Malfolded recombinant Tat substrates are Tat-independently degraded in Escherichia coli
AU - Lindenstrauß, Ute
AU - Matos, Cristina F.R.O.
AU - Graubner, Wenke
AU - Robinson, Colin
AU - Brüser, Thomas
N1 - Funding Information: This work has been supported by a grant of the Deutsche Forschungsgemeinschaft ( BR2285/1-3 ) to T.B. Copyright: Copyright 2010 Elsevier B.V., All rights reserved.
PY - 2010/8
Y1 - 2010/8
N2 - The twin-arginine translocation (Tat) system translocates folded proteins across biological membranes. It has been suggested that the Tat system of Escherichia coli can direct Tat substrates to degradation if they are not properly folded [Matos, C.F., Robinson, C. and Di Cola, A. (2008) The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J. 27, 2055-2063; Matos, C.F., Di Cola, A. and Robinson, C. (2009) TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli. EMBO Rep. 10, 474-479]. Contrary to the earlier reports, it is now concluded that reported differences between tested strains were due to variations in expression levels and inclusion body formation. Using the native Tat substrate NrfC and a malfolded variant thereof, we show that the turnover of these proteins is not affected by the absence of all known Tat components. Malfolded NrfC is degraded more quickly than the native protein, indicating that Tat-independent protease systems can recognize malfolded Tat substrates.
AB - The twin-arginine translocation (Tat) system translocates folded proteins across biological membranes. It has been suggested that the Tat system of Escherichia coli can direct Tat substrates to degradation if they are not properly folded [Matos, C.F., Robinson, C. and Di Cola, A. (2008) The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J. 27, 2055-2063; Matos, C.F., Di Cola, A. and Robinson, C. (2009) TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli. EMBO Rep. 10, 474-479]. Contrary to the earlier reports, it is now concluded that reported differences between tested strains were due to variations in expression levels and inclusion body formation. Using the native Tat substrate NrfC and a malfolded variant thereof, we show that the turnover of these proteins is not affected by the absence of all known Tat components. Malfolded NrfC is degraded more quickly than the native protein, indicating that Tat-independent protease systems can recognize malfolded Tat substrates.
KW - Protein degradation
KW - Protein folding
KW - Protein transport
KW - Quality control
KW - Twin-arginine translocation system
UR - http://www.scopus.com/inward/record.url?scp=77955655119&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2010.07.039
DO - 10.1016/j.febslet.2010.07.039
M3 - Article
C2 - 20659466
AN - SCOPUS:77955655119
VL - 584
SP - 3644
EP - 3648
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 16
ER -