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Novel Mitochondria-Targeted Heat-Soluble Proteins Identified in the Anhydrobiotic Tardigrade Improve Osmotic Tolerance of Human Cells
Open accessAbstract
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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“These abundantly expressed proteins included previously identified tardigrade-unique heat-soluble proteins, CAHS and SAHS, both of which maintain solubility even after heat treatment and are proposed to be involved in the protection of biomolecules during desiccation3132.”
From Extremotolerant tardigrade genome and improved radiotolerance of human cultured cells by tardigrade-unique protein (2016) · cites this paper as [32]
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Metadata
- Authors
- Tanaka, S., Tanaka, J., Miwa, Y., Horikawa, D. D., Katayama, T., Arakawa, K., Toyoda, A., Kubo, T., & Kunieda, T.
- Affiliations
- The University of Tokyo (JP)
- University of Tsukuba (JP)
- Keio University (JP)
- Database Center for Life Science (JP)
- National Institute of Genetics (JP)
- Corresponding author
- Kunieda, Takekazu
- ORCID
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-02-12
- Volume
- 10
- Issue
- 2
- Pages
- e0118272
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4326354
- OpenAlex
- W1964745114
- Cited by
- 128
- References
- 46
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 32 · 2023: 15 · 2022: 13 · 2021: 16 · 2020: 7 · 2019: 12 · 2018: 6 · 2017: 7 · 2016: 4 · 2015: 1
- FWCI
- 7.02
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology (No. 221S0002, 221S0002)
- Japan Society for the Promotion of Science (26660288, 25281016, 24657069, 13J10474, No. 221S0002, 221S0002)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Tardigrade Biology and Ecology
- Physical Sciences › Environmental Science › Ecology › Physiological and biochemical adaptations
- Physical Sciences › Environmental Science › Ecology › Polar Research and Ecology
- Keywords
- tardigrades, Ramazzottius varieornatus, anhydrobiosis, late embryogenesis abundant proteins, mitochondrial protection, desiccation tolerance, mitochondrial localization, human cells
- MeSH terms
- Amino Acid Sequence, Animals, Hot Temperature, Humans, Mitochondria, Molecular Sequence Data, Osmotic Pressure, Solubility, Amino Acid Motifs, Protein Transport, Mitochondrial Proteins, Tardigrada, Osmoregulation
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