The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.

@article{Pierpaoli1997ThePS,
  title={The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.},
  author={E V Pierpaoli and Erika Sandmeier and Antonio Baici and H J Schoenfeld and Simon Gisler and Philipp Christen},
  journal={Journal of molecular biology},
  year={1997},
  volume={269 5},
  pages={757-68}
}
The molecular chaperone DnaK, the Hsp70 homolog of Escherichia coli, acts in concert with the co-chaperones DnaJ and GrpE. The aim of this study was to identify the particular phase of the peptide binding-release cycle of the DnaK/DnaJ/GrpE system that is directly responsible for the chaperone effects. By real-time kinetic measurements of changes in the intrinsic fluorescence of DnaK and in the fluorescence of dansyl-labeled peptide ligands, the rates of the following steps in the chaperone… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 30 extracted citations

Thermosensitivity of growth is determined by chaperone-mediated proteome reallocation.

Proceedings of the National Academy of Sciences of the United States of America • 2017

Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.

Proceedings of the National Academy of Sciences of the United States of America • 2014
View 1 Excerpt

Similar Papers

Loading similar papers…