title: Trehalose is a versatile and long-lived chaperone for desiccation tolerance.
abstract: BACKGROUND
  Diverse organisms across taxa are desiccation tolerant, capable of surviving extreme water loss. Remarkably, desiccation tolerant organisms can survive years without water. However, the molecular mechanisms underlying this rare trait are poorly understood.
  
  
  RESULTS
  Here, using Saccharomyces cerevisiae, we show that intracellular trehalose is essential for survival to long-term desiccation. The time frame for maintaining long-term desiccation tolerance consists of a balance of trehalose stockpiled prior to desiccation and trehalose degradation by trehalases in desiccated cells. The activity of trehalases in desiccated cell reveals the stunning ability of cells to retain enzymatic activity while desiccated. Interestingly, the protein chaperone Hsp104 compensates for loss of trehalose during short-term, but not long-term, desiccation. We show that desiccation induces protein misfolding/aggregation of cytoplasmic and membrane proteins using luciferase and prion reporters. We demonstrate that trehalose, but not Hsp104, mitigates the aggregation of both cytoplasmic and membrane prions. We propose that desiccated cells initially accumulate both protein and chemical chaperones, like Hsp104 and trehalose, respectively. As desiccation extends, the activities of the protein chaperones are lost because of their complexity and requirement for energy, leaving trehalose as the major protector against the aggregation of cytoplasmic and membrane proteins.
  
  
  CONCLUSIONS
  Our results suggest that trehalose is both a more stable and more versatile protectant than protein chaperones, explaining its important role in desiccation tolerance and emphasizing the translational potential of small chemical chaperones as stress effectors.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
authors.forename: Hugo
authors.initials: H
authors.lastname: Tapia
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Electronic address: koshland@berkeley.edu.
authors.forename: Douglas E
authors.initials: DE
authors.lastname: Koshland
mesh_terms: D003681:Dehydration; D006360:Heat-Shock Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D014199:Trehalose / Q000378:metabolism*
chemical_list: D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae; D014199:Trehalose