Synergy between the small intrinsically disordered protein Hsp12 and trehalose sustain viability after severe desiccation.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30010539.
- Also identified by DOI 10.7554/eLife.38337 and PMC identifier 6054528.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Dehydration
- Heat-Shock Proteins
- Intrinsically Disordered Proteins
- Microbial Viability
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Stress, Physiological
- Trehalose