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Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

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Alternative bacterial two-component small heat shock protein systems.

Alexander Bepperling¹, Ferdinand Alte, Thomas Kriehuber

¹Department of Chemistry, Center for Integrated Protein Science, Technische Universität München, D-85748 Garching, Germany.

Proceedings of the National Academy of Sciences of the United States of America

|November 28, 2012

Summary

Small heat shock proteins (sHsps) prevent protein aggregation. This study reveals two Deinococcus radiodurans sHsps with distinct structures and functions, forming a novel bacterial chaperone system.

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Area of Science:

Molecular biology
Biochemistry
Structural biology

Background:

Small heat shock proteins (sHsps) are ATP-independent molecular chaperones crucial for preventing protein aggregation under stress.
Bacterial sHsp systems typically involve two homologous proteins, like in Escherichia coli (IbpA and IbpB).
Deinococcus radiodurans exhibits remarkable resistance to various stress conditions, including radiation and dehydration.

Purpose of the Study:

To investigate the structural and functional characteristics of the two small heat shock proteins (sHsps) in Deinococcus radiodurans.
To elucidate the oligomeric states and chaperone mechanisms of Hsp17.7 and Hsp20.2.
To determine if D. radiodurans represents a novel type of bacterial two-component sHsp system.

Main Methods:

Oligomeric state analysis of Hsp17.7 and Hsp20.2.
Chaperone activity assays to assess substrate binding and refolding capabilities.
Structural analysis, including X-ray crystallography, to determine the fold of Hsp17.7.

Main Results:

Hsp17.7 forms stable, chaperone-active dimers, despite possessing the canonical α-crystallin fold.
Hsp20.2 exists primarily as a large 36-mer that can dissociate into smaller, substrate-binding oligomers.
Hsp20.2 collaborates with ATP-dependent chaperones for protein refolding, while Hsp17.7 maintains substrates in a refolding-competent state via transient interactions.

Conclusions:

The two sHsps of Deinococcus radiodurans, Hsp17.7 and Hsp20.2, exhibit significant divergence in their quaternary structures and chaperone functions.
This functional and structural dichotomy suggests a second distinct type of bacterial two-component sHsp system.
The findings expand our understanding of bacterial chaperone diversity and stress response mechanisms.