Applied and Environmental Microbiology · 2012 · 13 citations · 17 references
Life SciencesMicrobiologyMolecular BiologyEnzymologyProtein FoldingMicrobial ProteomicsProtein DegradationProtein Folding PathwaysProtein RefoldingProteolytic EnzymesProteolytic ProcessingBacterial ProteasesExtracellular ProteasesMicrobial ProteasesProtease Cleavage SitesProtease Cleavage SpecificityProtease-mediated Protein DegradationProteolytic Degradation Of PeptidesSecreted Proteases
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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Two minimal Tat translocases in <i>Bacillus</i>
Jan D.H. Jongbloed, Ulrike Grieger, Haike Antelmann et al. · Molecular Microbiology · 2004 · 192 citations