Interaction of SecB with soluble SecA.
Copyright policy )Interaction of SecB with soluble SecA.
The preprotein binding molecular chaperone SecB functions by preventing the premature folding of the preprotein in the cytosol, and targeting it to the peripheral subunit SecA of the translocase at the cytoplasmic membrane. The nature of the interaction of SecB with soluble SecA was studied by fluorescence anisotropy spectroscopy of Ru(bpy)2(dcbpy)-labeled SecA in the presence of increasing concentrations of SecB. A more than 50-fold difference in affinity for the cytosolic SecA compared to translocase associated SecA seems to prevent unproductive binding of SecB to the cytosolic SecA and stresses its targeting function.
- University of Groningen Netherlands
SecA, PRECURSOR PROTEINS, Protein Folding, SecB, Light, Fluorescence Polarization, anisotropy, INNER MEMBRANE, Bacterial Proteins, Scattering, Radiation, CHAPERONE SECB, Adenosine Triphosphatases, SecA Proteins, TRIGGER FACTOR, Escherichia coli Proteins, Membrane Transport Proteins, COLI PLASMA-MEMBRANE, Rubidium, MOLECULAR CHAPERONES, ESCHERICHIA-COLI, PREPROTEIN TRANSLOCASE, PROTEIN TRANSLOCATION, SELECTIVE BINDING, preprotein targeting, SEC Translocation Channels, Protein Binding
SecA, PRECURSOR PROTEINS, Protein Folding, SecB, Light, Fluorescence Polarization, anisotropy, INNER MEMBRANE, Bacterial Proteins, Scattering, Radiation, CHAPERONE SECB, Adenosine Triphosphatases, SecA Proteins, TRIGGER FACTOR, Escherichia coli Proteins, Membrane Transport Proteins, COLI PLASMA-MEMBRANE, Rubidium, MOLECULAR CHAPERONES, ESCHERICHIA-COLI, PREPROTEIN TRANSLOCASE, PROTEIN TRANSLOCATION, SELECTIVE BINDING, preprotein targeting, SEC Translocation Channels, Protein Binding
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