ArticlePloS one2015
Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic Tardigrade improve osmotic tolerance of human cells.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 142 citations in OpenAlex.
- Tardigrade-Derived Strategy for Low-Cost Storage of Cell-Free Expression Lysates.ACS synthetic biology · 2026Article
- Diversifying particle-orientation distributions in cryo-EM with LEA protein additives.bioRxiv : the preprint server for biology · 2026Article
- Mitochondrial Abundant Heat Soluble (MAHS) Protein Expression Modulates Metabolic Dynamics in Human Adipose-Derived Stem Cells.International journal of molecular sciences · 2026Article
- At the Edge of Survival: Exploring the Frontiers of Tardigrade Extreme Stress Tolerance.Molecular ecology · 2026Review
- Expression of tardigrade extremotolerance-associated proteins improves recovery but not acute stress response of human microvascular endothelial cells.Scientific reports · 2026Article
- Integrative bioinformatics analysis of potential convergent evolution in tardigrade stress-response proteins.Stress biology · 2026Article
- Principles Underlying Cryopreservation and Freeze-Drying of Cells.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Surviving desiccation: key factors underlying tolerance in prokaryotes and eukaryotes.Protoplasma · 2025Review
- Article
- Possible roles of CAHS proteins from Tardigrade in osmotic stress tolerance in mammalian cells.Cell structure and function · 2024Article
- Search for putative gene regulatory motifs in CAHS3, linked to anhydrobiosis in a tardigrade Ramazzottius varieornatus, in vivo and in silico.Genes to cells : devoted to molecular & cellular mechanisms · 2024Article
- Metabolite phosphatase from anhydrobiotic tardigrades.The FEBS journal · 2024Article
- A bacterial expression cloning screen reveals single-stranded DNA-binding proteins as potent desicco-protectants.Cell reports · 2024Article
- An evaluation of thermal tolerance in six tardigrade species in an active and dry state.Biology open · 2024Article
- Structural study of the intrinsically disordered tardigrade damage suppressor protein (Dsup) and its complex with DNA.Scientific reports · 2024Article
- Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing.Nature communications · 2024Article
- Transcriptome analysis of the tardigrade Hypsibius exemplaris exposed to the DNA-damaging agent bleomycin.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Article
- Antioxidant Defense in the Toughest Animals on the Earth: Its Contribution to the Extreme Resistance of Tardigrades.International journal of molecular sciences · 2024Review
- Article
- Sexual dimorphism in the tardigrade Paramacrobiotus metropolitanus transcriptome.Zoological letters · 2024Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tardigrades are able to tolerate almost complete dehydration through transition to a metabolically inactive state, called "anhydrobiosis". Late Embryogenesis Abundant (LEA) proteins are heat-soluble proteins involved in the desiccation tolerance of many anhydrobiotic organisms. Tardigrades, Ramazzottius varieornatus, however, express predominantly tardigrade-unique heat-soluble proteins: CAHS (Cytoplasmic Abundant Heat Soluble) and SAHS (Secretory Abundant Heat Soluble) proteins, which are secreted or localized in most intracellular compartments, except the mitochondria. Although mitochondrial integrity is crucial to ensure cellular survival, protective molecules for mitochondria have remained elusive. Here, we identified two novel mitochondrial heat-soluble proteins, RvLEAM and MAHS (Mitochondrial Abundant Heat Soluble), as potent mitochondrial protectants from Ramazzottius varieornatus. RvLEAM is a group3 LEA protein and immunohistochemistry confirmed its mitochondrial localization in tardigrade cells. MAHS-green fluorescent protein fusion protein localized in human mitochondria and was heat-soluble in vitro, though no sequence similarity with other known proteins was found, and one region was conserved among tardigrades. Furthermore, we demonstrated that RvLEAM protein as well as MAHS protein improved the hyperosmotic tolerance of human cells. The findings of the present study revealed that tardigrade mitochondria contain at least two types of heat-soluble proteins that might have protective roles in water-deficient environments.
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