Zusammenfassung: | |
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.
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Lizenzbestimmungen: | Es gilt deutsches Urheberrecht. Das Dokument darf zum eigenen Gebrauch kostenfrei genutzt, aber nicht im Internet bereitgestellt oder an Außenstehende weitergegeben werden. Dieser Beitrag ist aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich. |
Publikationstyp: | Article |
Publikationsstatus: | publishedVersion |
Erstveröffentlichung: | 2014 |
Schlagwörter (englisch): | Membrane proteins, Protein transport, Protein-Protein interactions, Tat system, Twin-Arginine translocation, carrier protein, signal peptide, translocon, twin arginine translocation arresting protein A, twin arginine translocation arresting protein B, unclassified drug, arginine, carrier protein, Escherichia coli protein, TatA protein, E coli, TatB protein, E coli, article, carboxy terminal sequence, controlled study, in vivo study, membrane transport, molecular recognition, priority journal, protein cross linking, protein domain, chemical structure, metabolism, Arginine, Escherichia coli Proteins, Membrane Transport Proteins, Models, Molecular |
Fachliche Zuordnung (DDC): | 500 | Naturwissenschaften |
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