PMID:14580344
| Citation |
Alami, M, Lüke, I, Deitermann, S, Eisner, G, Koch, HG, Brunner, J and Müller, M (2003) Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12:937-46 |
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| Abstract |
The twin-arginine translocation (Tat) machinery of the Escherichia coli inner membrane is dedicated to the export of proteins harboring a conserved SRRxFLK motif in their signal sequence. TatA, TatB, and TatC are the functionally essential constituents of the Tat machinery, but their precise function is unknown. Using site-specific crosslinking, we have analyzed interactions of the twin-arginine precursor preSufI with the Tat proteins upon targeting to inner membrane vesicles. TatA association is observed only in the presence of a transmembrane H(+) gradient. TatB is found in contact with the entire signal sequence and adjacent parts of mature SufI. Interaction of TatC with preSufI is, however, restricted to a discrete area around the consensus motif. The results reveal a hierarchy in targeting of a Tat substrate such that for the primary interaction, TatC is both necessary and sufficient while a subsequent association with TatB likely mediates transfer from TatC to the actual Tat pore. |
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| Keywords |
Cell Membrane/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/physiology; Membrane Transport Proteins/metabolism; Membrane Transport Proteins/physiology; Protein Precursors/metabolism; Protein Sorting Signals/physiology; Protein Structure, Tertiary/physiology; Protein Transport/physiology; Protons; Signal Transduction/physiology; Transport Vesicles/metabolism |
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