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February 21, 2026Biophysical Journal0 citations

BPS2026 – Probing the evolution of desiccation resistance in tardigrade adenylate kinases

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YGYuling GuMPMark PetersenSMSusan Marqusee

Key Points

  • To investigate how tardigrade adenylate kinases have evolved to resist desiccation and their structural features.
  • Assembled an alignment of 30 tardigrade adenylate kinase sequences.
  • Analyzed phylogeny and constructed ancestral sequences for comparisons.
  • Expressed and purified specific tardigrade ADKs and compared their catalytic ability with E. coli ADK.
  • Identified conserved features in tardigrade ADKs like a 30-aa N-terminal insertion and an internal disulfide bridge.
  • Noted differences in surface chemistry compared to closely related species.
  • Planned future studies on recovery from desiccation and interactions with excipients.

Abstract

Tardigrades are a group of small invertebrates that can tolerate extreme deprivation of water (desiccation). While tardigrades produce certain intrinsically disordered proteins and sugars to act as excipients and aid protein recovery from desiccation, we hypothesize that their other proteins have also evolved to withstand desiccation. We assembled an alignment of 30 tardigrade adenylate kinase (ADK) sequences, analyzed their phylogeny and constructed ancestral sequences. We found some conserved features of tardigrade ADKs that are not observed in the ADKs of other closely related species: a 30-aa long N-terminal insertion, an internal disulfide bridge, and altered surface chemistry. We expressed and purified a subset of extant tardigrade ADKs and compared their catalytic ability with E. coli ADK, with future plans to investigate their recovery from desiccation and their interactions with excipients in the desiccated state.

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Cite This Study

Gu et al. (2026) studied this question.

synapsesocial.com/papers/69990e015b97ab4c14ac2f4fhttps://doi.org/10.1016/j.bpj.2025.11.1717
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