
Desiccation-related intrinsically disordered proteins (IDPs) from different organisms synergize best with their endogenous cosolutes to promote desiccation protection, and this synergy is mediated through distinct mechanisms between IDP families.


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The conformational ensemble and function of intrinsically disordered proteins (IDPs) are sensitive to their solution environment. The inherent malleability of disordered proteins combined with the exposure of their residues accounts for this sensitivity. One context in which IDPs play important roles that is concomitant with massive changes to the intracellular environment is during desiccation (extreme drying). The ability of organisms to survive desiccation has long been linked to the accumulation of high levels of cosolutes such as trehalose or sucrose as well as the enrichment of IDPs, such as late embryogenesis abundant (LEA) proteins or cytoplasmic abundant heat soluble (CAHS) proteins. Despite knowing that IDPs play important roles and are co-enriched alongside endogenous, species-specific cosolutes during desiccation, little is known mechanistically about how IDP-cosolute interactions influence desiccation tolerance. Here, we test the notion that the protective function of desiccation-related IDPs is enhanced through conformational changes induced by endogenous cosolutes. We find that desiccation-related IDPs derived from four different organisms spanning two LEA protein families and the CAHS protein family, synergize best with endogenous cosolutes during drying to promote desiccation protection. Yet the structural parameters of protective IDPs do not correlate with synergy for either CAHS or LEA proteins. We further demonstrate that for CAHS, but not LEA proteins, synergy is related to self-assembly and the formation of a gel. Our results demonstrate that functional synergy between IDPs and endogenous cosolutes is a convergent desiccation protection strategy seen among different IDP families and organisms, yet, the mechanisms underlying this synergy differ between IDP families.

### Competing Interest Statement

A.S.H. is a scientific consultant with Dewpoint Therapeutics and is on the Scientific Advisory Board of Prose Foods. The work reported here was not influenced by these affiliations. All other authors declare no competing interests.

Disordered proteins interact with the chemical environment to tune their protective function during drying

intrinsically-disordered-proteins-synergize-with-endogenous-cosolutes-to-enhance-desiccation-tolerance


Intrinsically Disordered Proteins Synergize with Endogenous Cosolutes to Enhance Desiccation Tolerance
