Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Bacillus subtilis / enzymology*
-
Bacillus subtilis / genetics
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism
-
Membrane Transport Proteins / genetics*
-
Membrane Transport Proteins / metabolism*
-
Peptide Hydrolases / genetics
-
Peptide Hydrolases / metabolism*
-
Peroxidases / chemistry
-
Peroxidases / genetics
-
Peroxidases / metabolism*
-
Protein Folding
-
Protein Transport
Substances
-
Bacterial Proteins
-
Membrane Transport Proteins
-
Peroxidases
-
Peptide Hydrolases