M. Muller, R.B. Klosgen, The Tat pathway in bacteria and chloroplasts (Review), Mol MembrMuller, M.; Bernd Klosgen, R. The Tat pathway in bacteria and chloroplasts (review). Mol. Membr. Biol., 2005, 22, 113-121.Muller M , Klosgen RB ( 2005 ) The Tat pathway in bacteria and ...
Both in prokaryotic organisms and in chloroplasts, a specialized protein transport pathway exists which is capable of translocating proteins in a fully folded conformation. Transport is mediated in both instances by signal peptides harbouring a twin-arginine consensus motif (twin-arginine translocation (...
B. The Tat pathway in bacteria and chloroplasts. Mol. Membrane Biol. 22, 113–121 (2005). Article Google Scholar Rollauer, S. E. et al. Structure of the TatC core of the twin-arginine protein transport system. Nature 492, 210–214 (2012). Article ADS CAS PubMed PubMed Central ...
(2002). Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J. Biol. Chem. 277, 29825–29831. Article PubMed CAS Google Scholar Douville, K., Price, A., Eichler, J., Economou, A., and Wickner, W. (1995). SecYEG and SecA are the stoichiometeric ...
Klösgen The Tat pathway in bacteria and chloroplasts Mol. Membr. Biol., 22 (2005), pp. 113-121 CrossrefView in ScopusGoogle Scholar 6 M.-R. Yen, Y.-H. Tseng, E.H. Nguyen, L.-F. Wu, M.H. Saier Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein ...
predicts the presence and location of Twin-arginine signal peptide cleavage sites in bacteria(细菌). The method incorporates a prediction of cleavage sites and a signal peptide/non-signal peptide prediction based on a combination of two artificial neural networks. A postfiltering of the output based...
The twin-arginine translocation (Tat) protein export system is present in the cytoplasmic membranes of most bacteria and archaea and has the highly unusual property of transporting fully folded proteins. The system must therefore provide a transmembrane pathway that is large enough to allow the ...
Due to this feature, the Tat pathway provides an attractive alternative to the secretory production of heterologous proteins via the Sec system. In this study, the potential for Tat-dependent heterologous protein secretion was compared in the three Gram-positive bacteria Staphylococcus carnosus, ...
The bacterial Tat protein translocation system is different with the Sec machinery which is general protein translocation system in the bacteria, but similar to ΔpH dependent pathway used for importing chloroplast proteins into the thylakoid. This system can export proteins with a twin arginine signal...
The twin arginine translocation pathway exports folded proteins across the cytoplasmic membrane of many bacteria. In Escherichia coli and other Gram-negative bacteria, TatA, TatB, and TatC are all essential for efficient translocation, and current models suggest that separate TatABC and TatA complexes ...