Release of both native and non-native proteins from a cis-only GroEL ternary complex

@article{Burston1996ReleaseOB,
  title={Release of both native and non-native proteins from a cis-only GroEL ternary complex},
  author={Steven G. Burston and Jonathan S. Weissman and George W. Farr and Wayne Fenton and Arthur L. Norwich},
  journal={Nature},
  year={1996},
  volume={383},
  pages={96-99}
}
PROTEIN folding by the double-ring chaperonin GroEL is initiated in cis ternary complexes, in which polypeptide is sequestered in the central channel of a GroEL ring, capped by the co-chaperonin GroES1–3. The cis ternary complex is dissociated (half-life of ˜15 s) by trans-sided ATP hydrolysis, which triggers release of GroES4–6. For the substrate protein rhodanese, only ˜15% of cis-localized molecules attain their native form before hydrolysis2,7. A major question concerning the GroEL… CONTINUE READING

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