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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
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Structural basis for intersubunit signaling in a protein disaggregating machine.

Amadeo B Biter1, Sukyeong Lee, Nuri Sung

  • 1Program in Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.

Proceedings of the National Academy of Sciences of the United States of America
|July 18, 2012
PubMed
Summary

ClpB protein disaggregase uses ATP energy for mechanical unfolding of protein aggregates. Its hexamer ring structure and ATP-dependent pore loop changes drive protein translocation, and deoligomerization is not required for its function.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • ClpB is an ATP-dependent protein disaggregase crucial for cellular protein homeostasis.
  • It functions with Hsp70 to refold aggregated proteins, but the mechanism of mechanical unfolding is not fully understood.

Purpose of the Study:

  • To elucidate the structural mechanism of ATP hydrolysis-driven protein unfolding by ClpB.
  • To understand the role of nucleotide binding and inter-subunit communication in ClpB function.

Main Methods:

  • X-ray crystallography of ClpB D2 domain.
  • Cryo-electron microscopy (cryo-EM) of the ClpB hexamer ring.
  • Biochemical assays to assess protein disaggregation activity.

Main Results:

  • Crystal structures reveal nucleotide-bound and -free states of the ClpB D2 domain.
  • Cryo-EM structure of the hexamer ring elucidates the ATP power stroke mechanism.
  • Pore loop conformation is coupled to nucleotide state and transmitted via inter-subunit signaling.
  • A disulfide-cross-linked ClpB hexamer remains fully functional, indicating deoligomerization is unnecessary.

Conclusions:

  • The study provides a structural basis for the ATP power stroke driving protein translocation through the ClpB hexamer.
  • ClpB utilizes a conserved AAA+ inter-subunit signaling pathway for mechanical unfolding.
  • ClpB disaggregation activity does not require its deoligomerization.