منابع مشابه
Assembling the Tat protein translocase
The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between th...
متن کاملRelaxed specificity of the Bacillus subtilis TatAdCd translocase in Tat-dependent protein secretion.
Protein translocation via the twin arginine translocation (TAT) pathway is characterized by the translocation of prefolded proteins across the hydrophobic lipid bilayer of the membrane. In Bacillus subtilis, two different Tat translocases are involved in this process, and both display different substrate specificities: PhoD is secreted via TatAdCd, whereas YwbN is secreted via TatAyCy. It was p...
متن کاملGenetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.
The twin arginine protein transport (Tat) system transports folded proteins across the cytoplasmic membranes of prokaryotes and the thylakoid membranes of plant chloroplasts. In Escherichia coli, the TatB and TatC components form a multivalent receptor complex that binds Tat substrates. Here, we have used a genetic fusion approach to construct covalent TatC oligomers in order to probe the organ...
متن کاملSubstrate-Dependent Assembly of the Tat Translocase as Observed in Live Escherichia coli Cells
The twin-arginine translocation (Tat) pathway guides fully folded proteins across membranes of bacteria, archaea and plant chloroplasts. In Escherichia coli, Tat-specific transport is executed in a still largely unknown manner by three functionally diverse membrane proteins, termed TatA, TatB, and TatC. In order to follow the intracellular distribution of the TatABC proteins in live E. coli cel...
متن کاملSubstrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly
The twin-arginine translocase (Tat) transports folded proteins across tightly sealed membranes. cpTatC is the core component of the thylakoid translocase and coordinates transport through interactions with the substrate signal peptide and other Tat components, notably the Tha4 pore-forming component. Here, Cys-Cys matching mapped Tha4 contact sites on cpTatC and assessed the role of signal pept...
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ژورنال
عنوان ژورنال: eLife
سال: 2016
ISSN: 2050-084X
DOI: 10.7554/elife.20718