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Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.

Huifang Hu1,2, Qing Wang2,3, Jingwen Du1,2

  • 1Analytical Research Center for Organic and Biological Molecules, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zu Chong Zhi Road, Shanghai 201203, China.

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Human Aha1, a co-chaperone for Hsp90, has distinct structural dynamics. Its N-terminal domain favors Hsp90 interaction, while the C-terminal domain stabilizes Hsp90. Both domains contribute to recognizing α-synuclein.

Keywords:
Aha1NMRchaperone-like activitydynamicsα-synuclein

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Chaperones

Background:

  • Aha1 is a crucial co-chaperone that stimulates Hsp90's ATPase activity.
  • Human Aha1 also possesses intrinsic chaperoning capabilities for stress-denatured proteins.
  • Understanding Aha1's structure and dynamics is key to elucidating its dual functions.

Purpose of the Study:

  • To investigate the structural and dynamic features of full-length human Aha1 using NMR.
  • To provide structural insights into Aha1's co-chaperone and chaperone-like activities.
  • To correlate structural properties with Aha1's functional roles in protein homeostasis.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the structure and dynamics of Aha1.
  • Thermal stability assays (melting temperature) for Aha1 domains.
  • Analysis of internal dynamics across various timescales (ps-ns and µs-ms).

Main Results:

  • Aha1's N-terminal domain (Aha1N) exhibits low thermal stability and slow dynamics, favoring interaction with Hsp90.
  • Aha1's C-terminal domain (Aha1C) shows high thermal stability and intermediate dynamics, suitable for stabilizing Hsp90.
  • The N-terminal region and C-terminal RLF motif of Aha1 are crucial for recognizing α-synuclein, despite lacking tight contacts.

Conclusions:

  • Distinct thermal stabilities and dynamics of Aha1 domains dictate their specific roles in Hsp90 interaction and stabilization.
  • Aha1N's inherent instability promotes binding to Hsp90, while Aha1C's stability supports Hsp90 complex formation.
  • Aha1's unique structural features enable its dual function as a co-chaperone and a recognition factor for pathological proteins like α-synuclein.