Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90.

@article{Shue1994StructuralAF,
  title={Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90.},
  author={Gongliang Shue and D. Stave Kohtz},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 4},
  pages={2707-11}
}
The assembly and folding of nascent polypeptides are mediated in vivo by molecular chaperones, many of which are members of the heat-shock family of proteins. We have shown previously that heat-shock protein 90 (HSP90) folds an inactive fraction of a recombinant basic helix-loop-helix (bHLH) protein generated in Escherichia coli (MyoD) into its active conformation. We show here that HSP90 also folds another bHLH protein (E12) and heterodimers of E12/MyoD into their active conformations. By… CONTINUE READING

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