Catapult mechanism renders the chaperone action of Hsp70 unidirectional.

@article{Gisler1998CatapultMR,
  title={Catapult mechanism renders the chaperone action of Hsp70 unidirectional.},
  author={Serge Mike Gisler and E V Pierpaoli and Philipp Christen},
  journal={Journal of molecular biology},
  year={1998},
  volume={279 4},
  pages={
          833-40
        }
}
Molecular chaperones of the Hsp70 type promote the folding and membrane translocation of proteins. The interaction of Hsp70s with polypeptides is linked to ATP binding and hydrolysis. We formed complexes of seven different fluorescence-labeled peptides with DnaK, the Hsp70 homolog of Escherichia coli, and determined the rate of peptide release under two different sets of conditions. (1) Upon addition of ATP to nucleotide-free peptide.DnaK complexes, all tested peptides were released with… CONTINUE READING

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