Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm.
The cysteines of the Escherichia coli periplasmic enzyme alkaline phosphatase, which are involved in disulfide bonds in the native enzyme, were found to be fully reduced when the protein was retained in the cytoplasm. Under these circumstances the cysteines remained reduced for at least several minutes after the synthesis of the protein was completed. This contrasted with the normally exported protein, wherein disulfide bonds formed rapidly. Disulfide bond formation accompanied export and processing. The implications of these findings for the inactivity of the enzyme in the cytoplasm are discussed.
Derman
A I
AI
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.
Beckwith
J
J
D000469:Alkaline Phosphatase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology; D004220:Disulfides / Q000032:analysis / Q000378:metabolism; D004229:Dithiothreitol / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007460:Iodoacetamide / Q000494:pharmacology; D007700:Kinetics; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational
D004220:Disulfides; D000469:Alkaline Phosphatase; D004229:Dithiothreitol; D007460:Iodoacetamide