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.</p
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Secretion of recombinant enzymes to extracellular milieu is important for enhanced degradation of to...
The twin-arginine translocation (Tat) pathway is known to translocate fully folded proteins across b...
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such prote...
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such prote...
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such prote...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Secretion of recombinant enzymes to extracellular milieu is important for enhanced degradation of to...
The twin-arginine translocation (Tat) pathway is known to translocate fully folded proteins across b...
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such prote...
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such prote...
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such prote...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export fr...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to e...
Secretion of recombinant enzymes to extracellular milieu is important for enhanced degradation of to...
The twin-arginine translocation (Tat) pathway is known to translocate fully folded proteins across b...