Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase in Escherichia coli.

ABSTRACT: Twin-arginine-dependent translocases transport folded proteins across bacterial, archaeal, and chloroplast membranes. Upon substrate binding, they assemble from hexahelical TatC and single-spanning TatA and TatB membrane proteins. Although structural and functional details of individual Tat subunits have been reported previously, the sequence and dynamics of Tat translocase assembly remain to be determined. Employing the zero-space cross-linker N,N'-dicyclohexylcarbodiimide (DCCD) in combination with LC-MS/MS, we identified as yet unknown intra- and intermolecular contact sites of TatB and TatC. In addition to their established intramembrane binding sites, both proteins were thus found to contact each other through the soluble N terminus of TatC and the interhelical linker re

SUBMITTER: Frobel J 

PROVIDER: S-EPMC6755809 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature