Tardígrados usam proteínas desordenadas intrinsecamente para sobreviver à dessecação

segunda-feira, março 20, 2017

Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation

Thomas C. Boothby 6, Thomas C. BoothbyEmail the author Thomas C. Boothby, Hugo Tapia, Alexandra H. Brozena, Samantha Piszkiewicz, Austin E. Smith, Ilaria Giovannini, Lorena Rebecchi, Gary J. Pielak, Doug Koshland, Bob Goldstein

6 Lead Contact

Article Information

Publication History

Published: March 16, 2017 Accepted: February 16, 2017 Received in revised form: December 14, 2016 

Received: July 26, 2016

Source/Fonte: The New York Times


• Tardigrade intrinsically disordered proteins (TDPs) are enriched during desiccation

• TDPs are required for tardigrades to survive desiccation

• Expression of TDPs increases desiccation tolerance in heterologous systems

• TDPs vitrify, and this vitrified state mirrors their protective capabilities


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.

Author Contributions

Conceptualization, (Lead) T.C.B. (supporting) B.G., G.J.P.; Investigation, T.C.B., H.T., A.H.B., S.P., A.E.S., I.G.; Resources, I.G., L.R., H.T., D.K.; Writing – Original Draft, T.C.B., S.P., G.J.P.; Writing – Review & Editing, T.C.B., H.T., A.H.B, S.P., A.E.S., I.G., L.R., G.J.P., D.K., B.G., Supervision, T.C.B., L.R., D.K., B.G., G.J.P.


This work was supported by NASA ( NNX15AB44G to T.C.B.) and the National Science Foundation ( MCB 1410854 and CHE 1607359 to G.J.P., IOS 1557432 and 1257320 to B.G.). L.R. and I.G. were supported by Young Researchers International Mobility of the University of Modena and Reggio Emilia and Fondo di Ateneo per la Ricerca (2015). We acknowledge the Harold and Leila Y. Mathers Charitable Foundation for supporting H.T. and the Simons Foundation of the Life Sciences Research Foundation for supporting T.C.B.

Received: July 26, 2016; Received in revised form: December 14, 2016; Accepted: February 16, 2017; Published: March 16, 2017

© 2017 Elsevier Inc.

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