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Related Experiment Videos

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

Clarissa L Weaver1, Elizabeth C Duran1, Korrie L Mack2

  • 1Department of Chemistry, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.

Biochemistry
|April 6, 2017
PubMed
Summary
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Heat shock protein 104 (Hsp104) disaggregation requires peptide binding, which is surprisingly only facilitated by ATPγS. This nucleotide-dependent peptide binding modulation is key to Hsp104

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Dynamics

Background:

  • Hsp104 is a crucial protein disaggregase involved in protein aggregate disruption.
  • Structural studies have proposed both planar and helical models for the hexameric Hsp104 structure.
  • Nucleotide ligation influences Hsp104 monomer conformation and hexamer formation.

Purpose of the Study:

  • To investigate the oligomeric state and peptide binding of Hsp104 without nucleotide and with various nucleotide analogs.
  • To determine the specific nucleotide conditions required for Hsp104's peptide binding competency.
  • To elucidate the role of nucleotide-dependent conformational changes in Hsp104's disaggregation mechanism.

Main Methods:

  • Analysis of Hsp104 oligomeric state under different nucleotide conditions.

Related Experiment Videos

  • Assessment of Hsp104 peptide binding affinity using various nucleotide analogs (ADP, ATPγS, AMPPNP, AMPPCP).
  • Comparison of peptide binding competency in the absence and presence of nucleotides.

    • Main Results:

    • Hsp104 exhibits varying peptide binding affinities depending on the nucleotide analog.
    • Only ATPγS was found to facilitate avid peptide binding by Hsp104.
    • Nucleotide-free conditions and other analogs (ADP, AMPPNP, AMPPCP) did not support strong peptide binding.

    Conclusions:

    • Nucleotide-dependent modulation of peptide binding affinity is critical for Hsp104 function.
    • The transition between high- and low-peptide affinity states, influenced by ATP analogs, is a key component of the protein disaggregation mechanism.
    • ATPγS plays a unique role in enabling Hsp104's avid peptide binding necessary for aggregate disruption.