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Molecular Chaperones and Protein Folding

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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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Modularity and intrinsic evolvability of Hsp90-buffered change.

Charles C Carey¹, Kristen F Gorman, Suzannah Rutherford

¹Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America.

|December 22, 2006

Summary

Heat shock protein 90 (Hsp90) allows hidden genetic variations to emerge during environmental stress. These Hsp90-buffered traits in Drosophila, like deformed eyes, were selectable without significant fitness costs.

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Area of Science:

Evolutionary biology
Developmental genetics

Background:

Heat shock protein 90 (Hsp90) influences phenotypic plasticity and is hypothesized to act as an evolutionary capacitor.
The role of Hsp90 in evolution is debated, particularly regarding whether Hsp90-buffered traits are unconditionally deleterious.

Purpose of the Study:

To investigate the fitness costs associated with Hsp90-buffered morphological abnormalities in Drosophila.
To determine if Hsp90-buffered traits, such as a deformed eye (dfe), incur correlated fitness deficits.

Main Methods:

Selection experiments were conducted on Drosophila lines with a dfe trait, varying its penetrance.
Fitness was assessed through viability, lifespan, and competitive fitness tests.
Quantitative Trait Loci (QTL) analysis was performed on recombinant lines to identify genes associated with dfe and fitness.

Main Results:

Despite significant variation in dfe penetrance (up to 120-fold), no measurable differences in viability, lifespan, or competitive fitness were observed.
Seventeen dfe QTL did not correlate with fitness effects in over 1,400 recombinant lines.
The study detected fitness effects of inbreeding, environment, and the white mutation independently of dfe penetrance.

Conclusions:

Large morphological changes controlled by Hsp90 can be selected for without significant, unconditional fitness costs.
Hsp90 buffers polygenic variation, allowing the substitution of deleterious alleles with less harmful ones that maintain similar phenotypes.
This supports the Hsp90 capacitor hypothesis, linking environmental stress to developmental variation and morphological plasticity.