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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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Small heat shock protein activity is regulated by variable oligomeric substructure.

Justin L P Benesch¹, Marina Ayoub, Carol V Robinson

¹Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.

The Journal of Biological Chemistry

|August 21, 2008

Summary

Alpha-crystallins, small heat shock proteins, shift from chaperone to aggregation adjuvant. Refolding studies reveal dimeric structure controls chaperone function, with monomeric bias linked to disease.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Alpha-crystallins are small heat shock proteins functioning as molecular chaperones.
They normally prevent protein aggregation but are implicated in protein deposition diseases.

Purpose of the Study:

Investigate quaternary structure changes in alpha-crystallins.
Understand the mechanism behind their switch from chaperone to aggregation adjuvant.

Main Methods:

Utilized novel mass spectrometry techniques.
Refolded alpha-crystallins in vitro to mimic post-translational modifications.
Analyzed oligomeric rearrangements and substrate affinity.

Main Results:

In vitro refolding induced oligomeric rearrangements without sequence alteration.
Loss of dimeric substructure correlated with increased substrate affinity.
Dimeric packaging regulates chaperone function by controlling hydrophobic surface exposure.

Conclusions:

Dimeric substructure in small heat shock proteins is crucial for controlling chaperone activity.
A shift towards monomeric substructure may underlie aberrant alpha-crystallin behavior in protein deposition diseases.