Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments

@article{Haslberger2008ProteinDB,
  title={Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments},
  author={Tobias Haslberger and Agnieszka Zdanowicz and Ingo L. Brand and Janine Kirstein and K{\"u}rşad Turgay and Axel Mogk and Bernd Bukau},
  journal={Nature Structural &Molecular Biology},
  year={2008},
  volume={15},
  pages={641-650}
}
The ring-forming AAA+ chaperone ClpB cooperates with the DnaK chaperone system to reactivate aggregated proteins. With the assistance of DnaK, ClpB extracts unfolded polypeptides from aggregates via substrate threading through its central channel. Here we analyze the processing of mixed aggregates consisting of protein fusions of misfolded and native domains. ClpB–DnaK reactivated all aggregated fusion proteins with similar efficiency, without unfolding native domains, demonstrating that… CONTINUE READING

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References

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recognition logic and operating principles

T. A. Baker, Sauer, R. T. ATP-dependent proteases of bacteria
Trends Biochem. Sci. 31, 647–653 • 2006

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