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 signal peptide of Bacillus subtilis YwbN can direct Tat-dependent secretion of methyl parathion hydrolase.
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College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, §Key Laboratory of Molecular Microbiology and Technology for Ministry of Education, Department of Microbiology, College of Life Sciences, and ¶Key Laboratory of Pollution Processes and Environmental Criteria for Ministry of Education, College of Environmental Science and Engineering, Nankai University, Tianjin 300071, People's Republic of China.
The twin-arginine translocation (Tat) pathway exports folded proteins across the cytoplasmic membranes of bacteria and archaea. Two parallel Tat pathways (TatAdCd and TatAyCy systems) with distinct substrate specificities have previously been discovered in Bacillus subtilis. In this study, to secrete methyl parathion hydrolase (MPH) into the growth medium, the twin-arginine signal peptide of B.
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Department of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to extracytoplasmic destinations. In recent years, most studies on bacterial Tat pathways addressed the membrane-bound TatA(B)C subunits of the Tat translocase, and the specific interactions between this translocase and its substrate proteins. In contrast, relatively few studies investigated possible coactors in the TatA(B)C-dependent protein translocation process.
View Article and Find Full Text PDFHigh-salinity growth conditions promote Tat-independent secretion of Tat substrates in Bacillus subtilis.
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Department of Medical Microbiology, University of Groningen and University Medical Center Groningen, Groningen, the Netherlands.
The Gram-positive bacterium Bacillus subtilis contains two Tat translocases, which can facilitate transport of folded proteins across the plasma membrane. Previous research has shown that Tat-dependent protein secretion in B. subtilis is a highly selective process and that heterologous proteins, such as the green fluorescent protein (GFP), are poor Tat substrates in this organism.
View Article and Find Full Text PDFDegradation of the twin-arginine translocation substrate YwbN by extracytoplasmic proteases of Bacillus subtilis.
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Department of Medical Microbiology, University of Groningen and University Medical Center Groningen, Groningen, the Netherlands.
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.
View Article and Find Full Text PDFEnvironmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.
PLoS One
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Department of Medical Microbiology, University Medical Center Groningen and University of Groningen, Groningen, The Netherlands.
Twin-arginine protein translocation (Tat) pathways are required for transport of folded proteins across bacterial, archaeal and chloroplast membranes. Recent studies indicate that Tat has evolved into a mainstream pathway for protein secretion in certain halophilic archaea, which thrive in highly saline environments. Here, we investigated the effects of environmental salinity on Tat-dependent protein secretion by the Gram-positive soil bacterium Bacillus subtilis, which encounters widely differing salt concentrations in its natural habitats.
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