title: Degradation of the twin-arginine translocation substrate YwbN by extracytoplasmic proteases of Bacillus subtilis.
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.
authors.affiliation: Department of Medical Microbiology, University of Groningen and University Medical Center Groningen, Groningen, the Netherlands.
authors.forename: Laxmi
authors.initials: L
authors.lastname: Krishnappa
authors.forename: Carmine G
authors.initials: CG
authors.lastname: Monteferrante
authors.forename: Jan Maarten
authors.initials: JM
authors.lastname: van Dijl
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000235:genetics* / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000235:genetics / Q000378:metabolism*; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding; D021381:Protein Transport
chemical_list: D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D010544:Peroxidases; D010447:Peptide Hydrolases