Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 52, Pages 21320-21329Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M117.812560
Keywords
Escherichia coli (E; coli); mass spectrometry (MS); membrane protein; protein cross-linking; protein export; protein targeting; Dicyclohexylcarbodiimide (DCCD; DCC); TatC; twin-arginine translocation
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Funding
- Deutsche Forschungsgemeinschaft [SFB 746, FOR 1905]
- Excellence Initiative of the German Federal & State Governments [GSC-4, EXC-294]
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Twin-arginine translocation (Tat) systems transport folded proteins across cellular membranes with the concerted action of mostly three membrane proteins: TatA, TatB, and TatC. Hetero-oligomers of TatB and TatC form circular substrate-receptor complexes with a central binding cavity for twin-arginine-containing signal peptides. After binding of the substrate, energy from an electro-chemical proton gradient is transduced into the recruitment of TatA oligomers and into the actual translocation event. We previously reported that Tat-dependent protein translocation into membrane vesicles of Escherichia coli is blocked by the compound N,N-dicyclohexylcarbodiimide (DCCD, DCC). We have now identified a highly conserved glutamate residue in the transmembrane region of E. coli TatC, which when modified by DCCD interferes with the deep insertion of a Tat signal peptide into the TatBC receptor complex. Our findings are consistent with a hydrophobic binding cavity formed by TatB and TatC inside the lipid bilayer. Moreover, we found that DCCD mediates discrete intramolecular cross-links of E. coli TatC involving both its N- and C-tails. These results confirm the close proximity of two distant sequence sections of TatC proposed to concertedly function as the primary docking site for twin-arginine signal peptides.
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