Chloramphenicol acetyltransferase, a cytoplasmic protein is incompatible for export from Bacillus subtilis.
Bacillus subtilis cells expressing a hybrid protein (Lvsss-Cat) consisting of the B. amyloliquefaciens levansucrase signal peptide fused to B. pumilus chloramphenicol acetyltransferase (Cat) are unable to export Cat protein into the growth medium. A series of tripartite protein fusions was constructed by inserting various lengths of the Cat sequences between the levansucrase signal peptide and staphylococcal protein A or Escherichia coli alkaline phosphatase. Biochemical characterization of the various Cat protein fusions revealed that multiple regions in the Cat protein were causing the export defect.
Chen
M W
MW
Central Research and Development Division, E. I. du Pont de Nemours Inc., Wilmington, Delaware 19880-0328.
Nagarajan
V
V
D001407:Bacillus / Q000201:enzymology / Q000235:genetics; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001692:Biological Transport; D015500:Chloramphenicol O-Acetyltransferase / Q000378:metabolism*; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000201:enzymology; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D015500:Chloramphenicol O-Acetyltransferase