The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

@article{Schoenfeld1995TheDC,
  title={The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.},
  author={H J Schoenfeld and Daniel P. Schmidt and Hartwig Schr{\"o}der and Bernd Bukau},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 5},
  pages={2183-9}
}
The DnaK (Hsp70), DnaJ, and GrpE heat shock proteins of Escherichia coli constitute a cellular chaperone system for protein folding. Substrate interactions are controlled by the ATPase activity of DnaK which itself is regulated by the nucleotide exchange factor GrpE. To understand the structure-function relationship of this chaperone system, the quaternary structures of DnaK, GrpE, and DnaK-GrpE complexes were analyzed by gel filtration chromatography, dynamic light scattering, analytical… CONTINUE READING
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