Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)*

@inproceedings{Kim2012SpecializedHC,
  title={Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)*},
  author={Jin Hae Kim and Marco Tonelli and Ronnie O. Frederick and Darius C.-F. Chow and John L. Markley},
  booktitle={The Journal of biological chemistry},
  year={2012}
}
The Escherichia coli protein IscU serves as the scaffold for Fe-S cluster assembly and the vehicle for Fe-S cluster transfer to acceptor proteins, such as apoferredoxin. IscU populates two conformational states in solution, a structured conformation (S) that resembles the conformation of the holoprotein IscU-[2Fe-2S] and a dynamically disordered conformation (D) that does not bind metal ions. NMR spectroscopic results presented here show that the specialized Hsp70 chaperone (HscA), alone or as… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 43 references

Similar Papers

Loading similar papers…