%0 Journal Article %1 blummelStructuralFeaturesTatC2017 %A Blümmel, Anne-Sophie %A Drepper, Friedel %A Knapp, Bettina %A Eimer, Ekaterina %A Warscheid, Bettina %A Müller, Matthias %A Fröbel, Julia %C United States %D 2017 %J The Journal of biological chemistry %K (DCCD (E. (MS),membrane Arginine/metabolism,Cell Binding,Protein Conformation,protein DCC),Dicyclohexylcarbodiimide/pharmacology,Escherichia Domains,protein Folding,Protein Hydrophilic Interactions,mass Membrane/metabolism,Crystallography Proteins/genetics/*metabolism,Escherichia Proteins/genetics/*metabolism,Protein Signals/physiology,protein Sorting Specificity,TatC,to_read,twin-arginine Transport X-Ray/methods,Dicyclohexylcarbodiimide and coli coli),Escherichia coli/metabolism,Hydrophobic cross-linking,Protein export,Protein protein,Membrane spectrometry targeting,Substrate translocation %N 52 %P 21320--21329 %R 10.1074/jbc.M117.812560 %T Structural Features of the TatC Membrane Protein That Determine Docking and Insertion of a Twin-Arginine Signal Peptide. %V 292 %X 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.

@article{blummelStructuralFeaturesTatC2017, 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.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {Bl{\"u}mmel, Anne-Sophie and Drepper, Friedel and Knapp, Bettina and Eimer, Ekaterina and Warscheid, Bettina and M{\"u}ller, Matthias and Fr{\"o}bel, Julia}, biburl = {https://www.bibsonomy.org/bibtex/2dc3cbfbbb74e5637fa0ce055b6416a6e/warscheidlab}, copyright = {{\copyright} 2017 by The American Society for Biochemistry and Molecular Biology, Inc.}, doi = {10.1074/jbc.M117.812560}, interhash = {4f47199d5c7786b0a6d622ffa6042745}, intrahash = {dc3cbfbbb74e5637fa0ce055b6416a6e}, issn = {1083-351X 0021-9258}, journal = {The Journal of biological chemistry}, keywords = {(DCCD (E. (MS),membrane Arginine/metabolism,Cell Binding,Protein Conformation,protein DCC),Dicyclohexylcarbodiimide/pharmacology,Escherichia Domains,protein Folding,Protein Hydrophilic Interactions,mass Membrane/metabolism,Crystallography Proteins/genetics/*metabolism,Escherichia Proteins/genetics/*metabolism,Protein Signals/physiology,protein Sorting Specificity,TatC,to_read,twin-arginine Transport X-Ray/methods,Dicyclohexylcarbodiimide and coli coli),Escherichia coli/metabolism,Hydrophobic cross-linking,Protein export,Protein protein,Membrane spectrometry targeting,Substrate translocation}, langid = {english}, month = dec, number = 52, pages = {21320--21329}, pmcid = {PMC5766949}, pmid = {29089385}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Structural Features of the {{TatC}} Membrane Protein That Determine Docking and Insertion of a Twin-Arginine Signal Peptide.}, volume = 292, year = 2017 }