Details
| Original language | English |
|---|---|
| Pages (from-to) | 827-836 |
| Number of pages | 10 |
| Journal | Biological Chemistry |
| Volume | 395 |
| Issue number | 7-8 |
| Publication status | Published - Jul 2014 |
Abstract
Tat systems translocate folded proteins across biological membranes of prokaryotes and plant plastids. TatBC complexes recognize N-Terminal Tat signal peptides that contain a sequence motif with two conserved arginines (RR-Motif), and transport takes place after a recruitment of TatA. Unfolded Tat substrate domains lower translocation efficiency and too long linkers lead to translocation arrest. To identify the components that interact with transported proteins during their passage through the translocon, we used a Tat substrate that arrests translocation at a long unfolded linker region, and we chose in vivo site-Directed photo cross-Linking to specifically detect the interactions of this linker region. For comparison, we included the interactions of the signal peptide and of the folded domain at the C-Terminus of this construct. The data show that the linker contacts only two, structurally similar Tat components, namely TatA and TatB. These contacts depend on the recognition of the Tat-Specific signal peptide. Only when membrane translocation of the globular domain was allowed - i.e., in the absence of the linker - we observed the same TatAB-Contacts also to the globular domain. The data thus suggest that mature protein domains are translocated through a TatAB environment.
Keywords
- Membrane proteins, Protein transport, Protein-Protein interactions, Tat system, Twin-Arginine translocation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
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In: Biological Chemistry, Vol. 395, No. 7-8, 07.2014, p. 827-836.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Twin-arginine translocation-arresting protein regions contact TatA and TatB
AU - Taubert, Johannes
AU - Brüser, Thomas
N1 - Funding Information: Acknowledgments: We thank Peter G. Schultz (The Scripps Research Institute, La Jolla) for donation of the pEVOL system, and Andrea Sinz and Christian Ihling (University of Halle-Wittenberg) for mass spectrometry analysis. This work was funded by the Deutsche Forschungsgemein-schaft (GRK 1026: ‘Conformational transitions during macromolecular interactions’). Copyright: Copyright 2014 Elsevier B.V., All rights reserved.
PY - 2014/7
Y1 - 2014/7
N2 - Tat systems translocate folded proteins across biological membranes of prokaryotes and plant plastids. TatBC complexes recognize N-Terminal Tat signal peptides that contain a sequence motif with two conserved arginines (RR-Motif), and transport takes place after a recruitment of TatA. Unfolded Tat substrate domains lower translocation efficiency and too long linkers lead to translocation arrest. To identify the components that interact with transported proteins during their passage through the translocon, we used a Tat substrate that arrests translocation at a long unfolded linker region, and we chose in vivo site-Directed photo cross-Linking to specifically detect the interactions of this linker region. For comparison, we included the interactions of the signal peptide and of the folded domain at the C-Terminus of this construct. The data show that the linker contacts only two, structurally similar Tat components, namely TatA and TatB. These contacts depend on the recognition of the Tat-Specific signal peptide. Only when membrane translocation of the globular domain was allowed - i.e., in the absence of the linker - we observed the same TatAB-Contacts also to the globular domain. The data thus suggest that mature protein domains are translocated through a TatAB environment.
AB - Tat systems translocate folded proteins across biological membranes of prokaryotes and plant plastids. TatBC complexes recognize N-Terminal Tat signal peptides that contain a sequence motif with two conserved arginines (RR-Motif), and transport takes place after a recruitment of TatA. Unfolded Tat substrate domains lower translocation efficiency and too long linkers lead to translocation arrest. To identify the components that interact with transported proteins during their passage through the translocon, we used a Tat substrate that arrests translocation at a long unfolded linker region, and we chose in vivo site-Directed photo cross-Linking to specifically detect the interactions of this linker region. For comparison, we included the interactions of the signal peptide and of the folded domain at the C-Terminus of this construct. The data show that the linker contacts only two, structurally similar Tat components, namely TatA and TatB. These contacts depend on the recognition of the Tat-Specific signal peptide. Only when membrane translocation of the globular domain was allowed - i.e., in the absence of the linker - we observed the same TatAB-Contacts also to the globular domain. The data thus suggest that mature protein domains are translocated through a TatAB environment.
KW - Membrane proteins
KW - Protein transport
KW - Protein-Protein interactions
KW - Tat system
KW - Twin-Arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=84904199609&partnerID=8YFLogxK
U2 - 10.1515/hsz-2014-0170
DO - 10.1515/hsz-2014-0170
M3 - Article
C2 - 25003386
AN - SCOPUS:84904199609
VL - 395
SP - 827
EP - 836
JO - Biological Chemistry
JF - Biological Chemistry
SN - 1431-6730
IS - 7-8
ER -