Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1.

@article{Qian2002DirectIB,
  title={Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1.},
  author={Xinguo Qian and Wenbo Hou and Li Zhengang and Bingdong Sha},
  journal={The Biochemical journal},
  year={2002},
  volume={361 Pt 1},
  pages={
          27-34
        }
}
Heat-shock protein 40 (Hsp40) enables Hsp70 to play critical roles in a number of cellular processes, such as protein folding, assembly, degradation and translocation in vivo. Hsp40 recognizes and binds non-native polypeptides and delivers them to Hsp70. Then Hsp40 stimulates the ATPase activity of Hsp70 to fold the polypeptides. By using yeast Hsp40 Sis1 and yeast Hsp70 Ssa1 as our model proteins, we found that the Sis1 peptide-binding fragment interacts directly with the full-length Ssa1 in… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 26 REFERENCES

of the peptide - binding fragment from the yeast Hsp 40 protein Sis 1

Z. Lu, D. M. Cyr
  • 1998

Structural analysis of substrate binding by the molecular chaperone

W. A. Hendrickson
  • DnaK. Science
  • 1996

Structural analysis of substrate binding by the molecular chaperone DnaK

K. M. Flaherty, C. DeLuca-Flaherty, D. B. McKay
  • Science
  • 1996