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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Nitration-driven structural changes in Hsp90 linked to gain of pathological functions.

Tilottama Chatterjee1, Alfonso Taboada2,3,4, Isabelle E Logan1,5

  • 1Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, U.S.A.

The Biochemical Journal
|July 30, 2025
PubMed
Summary

Protein tyrosine nitration alters heat shock protein 90 (Hsp90) structure and function. Site-specific nitration on Y33 or Y56 causes distinct pathological changes, impacting cellular processes and disease progression.

Keywords:
heat shock protein 90 (Hsp90)peroxynitritepost-translational modification (PTM)reactive nitrogen species (RNS)structure-functiontyrosine nitration

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein tyrosine nitration is an oxidative modification implicated in diseases like neurodegenerative disorders and cancer.
  • Nitration of specific tyrosine residues in heat shock protein 90 (Hsp90) can lead to pathological gain-of-function.
  • Previous work demonstrated distinct cellular effects of Hsp90 nitrated at Y33 (mitochondrial dysfunction) versus Y56 (P2X7 receptor activation).

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying site-specific Hsp90 nitration.
  • To investigate the structural and functional consequences of Hsp90 nitration at Y33 and Y56.
  • To establish a foundation for developing targeted therapies against pathological Hsp90 variants.

Main Methods:

  • Biophysical assays
  • Biochemical analyses
  • In silico molecular dynamics simulations

Main Results:

  • Nitration at Y33 and Y56 induces significant, site-dependent structural changes in Hsp90.
  • Nitration destabilizes the Hsp90 dimer, promoting the formation of stable oligomeric species.
  • Differential impacts on Hsp90 ATPase and holdase activities were observed based on the nitrated residue (Y33 vs. Y56).
  • Molecular dynamics simulations revealed nitration's effect on ATP-lid dynamics and ATP-R392 interactions, crucial for ATPase activity.

Conclusions:

  • Hsp90 nitration at Y33 and Y56 triggers distinct structural alterations, impacting its enzymatic and chaperone functions.
  • These site-specific modifications contribute to disease-driving functions.
  • Understanding these molecular changes is essential for developing targeted therapeutic strategies against aberrant Hsp90 activity in disease.