Mechanistic analysis of the minimalistic twin-arginine translocation system found in Bacillus subtilis
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چکیده
منابع مشابه
Degradation of the twin-arginine translocation substrate YwbN by extracytoplasmic proteases of Bacillus subtilis.
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such proteins are usually resistant to proteolysis. Here we show that multiple extracellular proteases degrade the B. subtilis Tat substrate YwbN. This suggests either that secreted YwbN is not fully folded or that folded YwbN exposes protease cleavage sites.
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Twin arginine translocation (Tat) systems catalyze the transport of folded proteins across the bacterial cytosolic membrane or the chloroplast thylakoid membrane. In the Tat systems of Escherichia coli and many other species TatA-, TatB-, and TatC-like proteins have been identified as essential translocase components. In contrast, the Bacillus subtilis phosphodiesterase PhoD-specific system con...
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recombinant protein production in e. coli has several advantages over other expression systems. misfolding, inclusion body formation, and lack of eukaryotic post translational modification are the most disadvantages of this system. exporting of correctly folded proteins to the outside of reductive cytoplasmic environment through twin-arginine system could help to pass these limiting steps. two ...
متن کاملThe archaeal twin-arginine translocation pathway.
The twin-arginine translocation (Tat) pathway is a system with the unique ability to export proteins in a fully folded conformation. Its main components are TatA, TatB and TatC, all of which are required for Tat-dependent export. The Tat pathway is found in several Archaea, and in most of them a moderate number of predicted Tat-dependent substrates are present. Putative substrates include those...
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ژورنال
عنوان ژورنال: Access Microbiology
سال: 2019
ISSN: 2516-8290
DOI: 10.1099/acmi.ac2019.po0183