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Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.

Emma E Cawood1, G Marius Clore2, Theodoros K Karamanos1

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|March 5, 2022
PubMed
Summary

The T193A mutation in DNAJB6 (a chaperone protein) increases partially folded states, impacting its oligomerization and anti-aggregation activity. This finding links chaperone dynamics to Parkinson's disease, suggesting new therapeutic targets.

Keywords:
Hsp40 ChaperonesOligomerizationProtein Correlated MotionsProtein DynamicsProtein Excited StatesRelaxation-Based NMR

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • DNAJB6 is an anti-aggregation chaperone functioning as a dynamic oligomer.
  • Subunit exchange in DNAJB6 oligomers is crucial for inhibiting client protein aggregation.
  • A T193A mutation in DNAJB6's C-terminal domain (CTD) impairs self-oligomerization and anti-aggregation, and is linked to Parkinson's disease.

Purpose of the Study:

  • To investigate the structural and dynamic effects of the T193A mutation on the DNAJB6 CTD.
  • To understand how the T193A mutation affects DNAJB6's oligomerization and chaperone activity.
  • To explore the link between DNAJB6 dynamics, oligomerization, and anti-aggregation in the context of Parkinson's disease.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Relaxation-based NMR methods.
  • Analysis of protein structure and dynamics.

Main Results:

  • The T193A mutation minimally impacts the β-stranded CTD structure.
  • The mutation increases the population and formation rate of a partially folded state.
  • These changes are attributed to β-strand peptide plane flips, altering CTD oligomerization and anti-aggregation capabilities.

Conclusions:

  • Chaperone dynamics, specifically CTD pleat/flatness changes driven by peptide plane flips, are critical for DNAJB6 oligomerization and anti-aggregation.
  • The T193A mutation disrupts these dynamics, providing a molecular link to Parkinson's disease.
  • Understanding these mechanisms may pave the way for novel therapeutic strategies targeting specific substrates.