Trehalose is a versatile and long-lived chaperone for desiccation tolerance

Area of Science:

• Biochemistry
• Cell Biology
• Molecular Biology

Background:

• Desiccation tolerance is a rare trait enabling organisms to survive extreme water loss.
• The molecular basis of desiccation tolerance remains largely unknown.

Purpose of the Study:

• To investigate the molecular mechanisms of long-term desiccation tolerance in Saccharomyces cerevisiae.
• To elucidate the roles of trehalose and protein chaperones in cellular protection during dehydration.

Main Methods:

• Utilized Saccharomyces cerevisiae as a model organism.
• Employed luciferase and prion reporters to assess protein misfolding and aggregation.
• Investigated the activity of trehalases and the function of Hsp104 under desiccated conditions.

Main Results:

• Intracellular trehalose is essential for long-term desiccation survival.
• Trehalose degradation by trehalases occurs in desiccated cells, balancing stockpiled reserves.
• Hsp104 (a protein chaperone) aids short-term but not long-term desiccation tolerance.
• Trehalose mitigates both cytoplasmic and membrane protein aggregation, unlike Hsp104.
• Desiccation induces protein misfolding and aggregation.

Conclusions:

• Trehalose is a more stable and versatile protectant than protein chaperones during prolonged desiccation.
• Trehalose's efficacy highlights its critical role in desiccation tolerance.
• Small chemical chaperones like trehalose show translational potential as stress effectors.