Hartwig Schröder

TL;DR: The protein repair function of DnaK, GrpE and, in particular, DnaJ is likely to be part of the role of these proteins in regulation of the heat shock response.

TL;DR: A model reaction in which DnaK, DnaJ, and GrpE mediate the folding of denatured firefly luciferase is analyzed to gain a biologically relevant understanding of the mechanism of Hsp70 action.

TL;DR: In this article, the authors analyzed mutants of DnaK, an Hsp70 homolog, altered in key residues of its substrate binding domain and found that the conformational changes in the alpha-helical lid and the beta-domain caused the opening of the substrate binding cavity.

TL;DR: Fluorescence analysis of the N-terminally located single tryptophan residue of DnaK revealed that the known ATP-induced alteration of the emission spectrum, proposed to result directly from conformational changes in the ATPase domain, requires the presence of the C-terminal domain and therefore mainly results from altered domain interaction.

TL;DR: It is shown for the Escherichia coli Hsp70 homolog, DnaK, that stimulation by DnaJ requires the linked ATPase and substrate-binding domains of Dna k, and evolutionary conservation of the channel and the J-domain suggests conservation ofThe mechanism of action of DNAJ proteins.