Tardigrades took a protein normally used for 'trash pickup' and turned it into a permanent, bulletproof bodyguard for their DNA.
April 13, 2026
Original Paper
Cryo-EM structures of a neofunctionalized tardigrade peroxiredoxin specialized for nucleic acid binding
bioRxiv · 10.64898/2026.04.10.717662
The Takeaway
These nearly indestructible creatures evolved a version of an antioxidant protein that stopped fighting chemicals and started physically protecting the cell's nucleus. It's a bizarre example of evolution completely changing a protein's day job to survive extreme stress.
From the abstract
Some terrestrial tardigrades can endure severe oxidative stress in part through their gene-expanded repertoire of antioxidant proteins. However, among these antioxidant proteins, RvPrxL, a peroxiredoxin (Prx)-like protein from Ramazzottius varieornatus strain YOKOZUNA-1, is unusual in that the catalytic cysteine is replaced by glutamate, apparently incapacitating canonical peroxidase function. In this study, we investigated the structure and function of this atypical Prx. Biochemical assays demo