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Interaction of SecB with soluble SecA 1
Author(s) -
den Blaauwen Tanneke,
Terpetschnig Ewald,
Lakowicz Joseph R,
Driessen Arnold J.M
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01142-3
Subject(s) - translocase , cytosol , cytoplasm , biophysics , fluorescence anisotropy , chaperone (clinical) , protein subunit , biochemistry , chemistry , membrane , biology , chromosomal translocation , enzyme , medicine , pathology , gene
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.