PMID:11923313

Citation	Alami, M, Trescher, D, Wu, LF and Müller, M (2002) Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J. Biol. Chem. 277:20499-503
Abstract	The twin-arginine translocation (Tat) pathway exports those precursor proteins to the periplasmic space of bacteria that harbor a twin-arginine (RR) consensus motif in their signal sequences. We have reproduced translocation of several Tat substrates into inside-out plasma membrane vesicles from Escherichia coli. Translocation proceeding at an efficiency of up to 20% occurs specifically via the Tat pathway as indicated by (i) its requirement for elevated levels of the TatABC proteins in the membrane vesicles, (ii) competition by an intact twin-arginine signal peptide, and (iii) susceptibility toward dissipation of the transmembrane H(+) gradient. The latter treatment, while blocking translocation, still allows for functional membrane association of Tat precursors. This is shown by the finding that translocation of isolated membrane-bound Tat precursor is restored upon re-energization of the vesicles.
Links	PubMed Online version:10.1074/jbc.M201711200
Keywords	Amino Acid Sequence; Base Sequence; DNA Primers; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/metabolism; Molecular Sequence Data; Protein Binding; Protein Transport
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