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Elife. 2019 Oct 1;8. pii: e47682. doi: 10.7554/eLife.47682.

The tardigrade damage suppressor protein binds to nucleosomes and protects DNA from hydroxyl radicals.

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Section of Molecular Biology, University of California, San Diego, San Diego, United States.
Contributed equally


Tardigrades, also known as water bears, are animals that can survive extreme conditions. The tardigrade Ramazzottius varieornatus contains a unique nuclear protein termed Dsup, for damage suppressor, which can increase the resistance of human cells to DNA damage under conditions, such as ionizing radiation or hydrogen peroxide treatment, that generate hydroxyl radicals. Here we find that R. varieornatus Dsup is a nucleosome-binding protein that protects chromatin from hydroxyl radicals. Moreover, a Dsup ortholog from the tardigrade Hypsibius exemplaris similarly binds to nucleosomes and protects DNA from hydroxyl radicals. Strikingly, a conserved region in Dsup proteins exhibits sequence similarity to the nucleosome-binding domain of vertebrate HMGN proteins and is functionally important for nucleosome binding and hydroxyl radical protection. These findings suggest that Dsup promotes the survival of tardigrades under diverse conditions by a direct mechanism that involves binding to nucleosomes and protecting chromosomal DNA from hydroxyl radicals.


Ramazzottius varieornatus; chromatin; chromosomes; damage suppressor protein; gene expression; hydroxyl radicals; nucleosome; tardigrade

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