Synergy between the small intrinsically disordered protein Hsp12 and trehalose sustain viability after severe desiccation

Elife. 2018 Jul 16:7:e38337. doi: 10.7554/eLife.38337.

Abstract

Anhydrobiotes are rare microbes, plants and animals that tolerate severe water loss. Understanding the molecular basis for their desiccation tolerance may provide novel insights into stress biology and critical tools for engineering drought-tolerant crops. Using the anhydrobiote, budding yeast, we show that trehalose and Hsp12, a small intrinsically disordered protein (sIDP) of the hydrophilin family, synergize to mitigate completely the inviability caused by the lethal stresses of desiccation. We show that these two molecules help to stabilize the activity and prevent aggregation of model proteins both in vivo and in vitro. We also identify a novel in vitro role for Hsp12 as a membrane remodeler, a protective feature not shared by another yeast hydrophilin, suggesting that sIDPs have distinct biological functions.

Keywords: Hsp12; S. cerevisiae; biochemistry; cell biology; chemical biology; desiccation tolerance; sIDP; trehalose.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / metabolism
  • Dehydration*
  • Heat-Shock Proteins / metabolism*
  • Intrinsically Disordered Proteins / metabolism*
  • Microbial Viability*
  • Protein Aggregation, Pathological / prevention & control
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Stress, Physiological*
  • Trehalose / metabolism*

Substances

  • HSP12 protein, S cerevisiae
  • Heat-Shock Proteins
  • Intrinsically Disordered Proteins
  • Saccharomyces cerevisiae Proteins
  • Trehalose