Journal Article10.1016/S0022-2836(02)00820-3
Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
Erik de Leeuw,Thierry Granjon,Ida Porcelli,Meriem Alami,Stephen B. Carr,Matthias Müller,Frank Sargent,Tracy Palmer,Tracy Palmer,Ben C. Berks +9 more
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TL;DR: The authors' data suggest that the TatA, TatB and TatC proteins are found in at least two major types of high molecular mass complex in detergent solution, one consisting predominantly of TatA but with a small quantity of TatB, and the other based on a TatBC unit but also containing some TatA protein.
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About: This article is published in Journal of Molecular Biology. The article was published on 04 Oct 2002. The article focuses on the topics: Twin-arginine translocation pathway & Signal peptide.
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Citations
Moving folded proteins across the bacterial cell membrane.
TL;DR: The Tat translocase faces the formidable challenge of moving structured macromolecular substrates across the bacterial cytoplasmic membrane without rendering the membrane freely permeable to protons and other ions.
111
Topological studies on the twin-arginine translocase component TatC.
TL;DR: Studies with translational fusions of TatC to the topological marker enzymes PhoA and LacZ provide strong evidence for a six-trans-membrane domain topology, and point to the importance of cytoplasmic loops for the stabilization of stop-transfer sequences and revoke evidence for only four trans- Membrane domains of Tat C.
83
Dual Topology of the Escherichia coli TatA Protein
TL;DR: In vitro and in vivo proteolysis assay showed that the Tcs site of TatAT53::Tcs was accessible from both the periplasm and cytoplasm, indicating a dual topology of the TatA C terminus, and its implication in protein transport is discussed.
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Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy.
TL;DR: Interestingly, the APH showed an unexpectedly slanted alignment in the protein, different from that of the isolated APH peptide, which implies that the amphiphilic region of TatA is not just a flexible attachment to the transmembrane anchor but might be able to form intra- or even intermolecular salt-bridges, which could play a key role in pore assembly.
77
Constructing the wonders of the bacterial world: biosynthesis of complex enzymes
TL;DR: Recent descriptions of a chaperone-mediated 'proofreading' system involved in coordinating assembly and export of complex extracellular enzymes will be discussed, focusing on the molybdenum-containing respiratory enzymes central to anaerobic respiration in Escherichia coli.
77
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