Lactose-Specific Enzyme II of the Phosphoenol Pyruvate-Dependent Phosphotransferase System of Staphylococcus aureus
作者： Dirk Peters , Rainer Frank , Wolfgang Hengstenberg
DOI: 10.1111/J.1432-1033.1995.0798M.X
关键词:
摘要: The lactose-specific integral-membrane-protein enzyme II (IICBLac) of the bacterial phosphoenolpy-ruvate-dependent phosphotransferase system Staphylococcus aureus catalyses uptake and phosphorylation lactose. It consists an N-terminal membrane-spanning IIC domain a C-terminal hydrophilic IIB domain. IICBLac was fused with tag six histidine residues using recombinant DNA technology. resulting protein, IICBLac-His, produced in Escherichia coli purified under non-denaturing conditions to homogenity. purification procedure consits NaOH extraction step followed by solubilisation Triton X-100, metal-affinity chromatography Ni2+-nitrilotriacetic acid resin. His-tagged protein possessed subtrate specifity identical that wild-type protein. To investigate domain, sequence coding for His were in-frame specific initiation signal. overproduced IIBLac-His obtained pure form. Bacterial phospho-transferase-system-dependent IIB-His demonstrated photometric assay urea/polyacrylamide gel electrophoresis. activity mutant [C476S]-IICB1, containing mutagenized site, restored presence assay.
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