Unknown

Dataset Information

0

Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.


ABSTRACT: 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.

SUBMITTER: Blummel AS 

PROVIDER: S-EPMC5766949 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.

Blümmel Anne-Sophie AS   Drepper Friedel F   Knapp Bettina B   Eimer Ekaterina E   Warscheid Bettina B   Müller Matthias M   Fröbel Julia J  

The Journal of biological chemistry 20171031 52


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 eve  ...[more]

Similar Datasets

| S-EPMC3538955 | biostudies-literature
| S-EPMC2661573 | biostudies-literature
| S-EPMC3653977 | biostudies-literature
| S-EPMC2000414 | biostudies-literature
| S-EPMC3573685 | biostudies-literature
| S-EPMC5539426 | biostudies-other
| S-EPMC5102672 | biostudies-literature
| S-EPMC3712460 | biostudies-literature
| S-EPMC3903283 | biostudies-literature
| S-EPMC3383694 | biostudies-other