Journal
FEBS LETTERS
Volume 497, Issue 1, Pages 55-58Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)02435-8
Keywords
molecular chaperone; DnaK; DnaJ; Hsp70; Hsp40; oligomerization
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Hsp70s assist the folding of proteins in an ATP-dependent manner. DnaK, the Hsp70 of Escherichia coli, acts in concert with its co-chaperones DnaJ and GrpE, Amino acid substitutions (D388R and L391S/L392G) in the linker region between the ATPase and substrate-binding domain did not affect the functional domain coupling and oligomerization of DnaK, The intrinsic ATPase activity was enhanced up to 10-fold, However, the ATPase activity of DnaK L391S/L392G, if stimulated by DnaJ plus protein substrate, was five times lower than that of wild-type DnaK and DnaK D388R, This defect correlated with the complete loss of chaperone action in luciferase refolding, Apparently, the conserved leucine residues in the linker mediate the synergistic effects of DnaJ and protein substrate on ATPase activity, a function which might be essential for chaperone action, (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B,V, All rights reserved.
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