Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

@article{Buchberger1996SubstrateSB,
  title={Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.},
  author={Alexander Buchberger and Hartwig Schr{\"o}der and Thomas Hesterkamp and H J Schoenfeld and Bernd Bukau},
  journal={Journal of molecular biology},
  year={1996},
  volume={261 3},
  pages={328-33}
}
GroEL and DnaK with their cofactors constitute the major chaperone systems promoting protein folding in the Escherichia coli cytosol. The ability of GroEL to bind and promote folding of a substrate released from DnaK led to the proposal that the DnaK and GroEL systems act successively along a protein folding pathway. Here we have investigated the role of both systems in preventing aggregation and assisting refolding of firefly luciferase denatured by guanidinium chloride and heat. We find that… CONTINUE READING
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