4.8 Article

Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation

期刊

MOLECULAR CELL
卷 65, 期 6, 页码 975-+

出版社

CELL PRESS
DOI: 10.1016/j.molcel.2017.02.018

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资金

  1. NASA [NNX15AB44G]
  2. National Science Foundation [MCB 1410854, CHE 1607359, IOS 1557432, 1257320]
  3. University of Modena
  4. Reggio Emilia
  5. Fondo di Ateneo per la Ricerca
  6. Harold and Leila Y. Mathers Charitable Foundation
  7. Simons Foundation of the Life Sciences Research Foundation
  8. NASA [NNX15AB44G, 808401] Funding Source: Federal RePORTER
  9. Direct For Biological Sciences
  10. Division Of Integrative Organismal Systems [1557432, 1257320] Funding Source: National Science Foundation
  11. Direct For Mathematical & Physical Scien
  12. Division Of Chemistry [1607359] Funding Source: National Science Foundation
  13. Div Of Molecular and Cellular Bioscience
  14. Direct For Biological Sciences [1410854] Funding Source: National Science Foundation

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Tardigrades are microscopic animals that survive a remarkable array of stresses, including desiccation. How tardigrades survive desiccation has remained a mystery for more than 250 years. Trehalose, a disaccharide essential for several organisms to survive drying, is detected at low levels or not at all in some tardigrade species, indicating that tardigrades possess potentially novel mechanisms for surviving desiccation. Here we show that tardigrade-specific intrinsically disordered proteins (TDPs) are essential for desiccation tolerance. TDP genes are constitutively expressed at high levels or induced during desiccation in multiple tardigrade species. TDPs are required for tardigrade desiccation tolerance, and these genes are sufficient to increase desiccation tolerance when expressed in heterologous systems. TDPs form non-crystalline amorphous solids (vitrify) upon desiccation, and this vitrified state mirrors their protective capabilities. Our study identifies TDPs as functional mediators of tardigrade desiccation tolerance, expanding our knowledge of the roles and diversity of disordered proteins involved in stress tolerance.

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