DnaJ-promoted binding of DnaK to multiple sites on σ32 in the presence of ATP.

@article{Noguchi2014DnaJpromotedBO,
  title={DnaJ-promoted binding of DnaK to multiple sites on σ32 in the presence of ATP.},
  author={Aki Noguchi and Ayami Ikeda and Moeka Mezaki and Yoshihiro Fukumori and Masaaki Kanemori},
  journal={Journal of bacteriology},
  year={2014},
  volume={196 9},
  pages={1694-703}
}
The Escherichia coli DnaK chaperone system is a canonical heat shock protein 70 (Hsp70) chaperone system comprising Hsp70, Hsp40, and a nucleotide exchange factor. Although Hsp40 is known to facilitate the effective binding of Hsp70 to substrates, the role of Hsp40 in Hsp70-substrate interactions has not yet been fully elucidated. Using the E. coli heat shock transcription factor σ(32) as a substrate in the DnaK chaperone system, we here provide new insight into the Hsp70-substrate interaction… CONTINUE READING
5 Citations
39 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 39 references

Similar Papers

Loading similar papers…