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Papers In Press, published online ahead of print July 25, 2000
Department of Biology, Johns Hopkins University, Baltimore, MD 21218
Corresponding Author: roseman{at}jhu.edu
The phosphoenolpyruvate: glycose transferase system (PTS) is a prototypic signaling system responsible for the vectorial uptake and phosphorylation of carbohydrate substrates. The accompanying papers describe the proteins and product of the Escherichia coli N,N-diacetylchitobiose [(GlcNAc)2] PTS mediated permease. Unlike most PTS transporters, the Chb system is composed of two soluble proteins, IIAChb and IIBChb, and one transmembrane receptor (IICChb). The oligomeric states of PTS permease proteins and phosphoproteins have been difficult to determine. Using analytical ultracentrifugation, both dephospho and phosphorylated-IIAChb are shown to exist as stable dimers, while IIBChb, phospho-IIBChb and the mutant (Cys10Ser)IIBChb are monomers. The mutant protein (Cys10Ser)IIBChb is unable to accept phosphate from phospho-IIAChb, but forms a stable higher order complex with phospho-IIAChb (but not with dephospho-IIAChb). The stoichiometry of proteins in the purified complex was determined to be 1:1 indicating that 2 molecules of (Cys10Ser)IIBChb are associated with one phospho-IIAChb dimer in the complex. The complex appears to be a transition state analogue in the phosphotransfer reaction between the proteins. A model is presented that describes the concerted assembly and disassembly of IIAChb:IIBChb complexes contingent on phosphorylation-dependent conformational changes, especially of IIAChb.
J. Biol. Chem, 10.1074/jbc.M001717200
Submitted on March 2, 2000
Revised on May 25, 2000
Accepted on July 25, 2000
Characterization of the IIAChb and IIBChb Proteins of the Escherichia coli N,N'-Diacetylchitobiose Phosphotransferase System by Analytical Sedimentation: Formation of a Model Phosphotransfer Transition State Complex
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