Tardigrade specific proteins

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Tardigrade specific proteins (TDPs) are specific types of Intrinsically Disordered Proteins (IDPs) that are seen in tardigrades. They are most notably used to help them survive desiccation which makes them very extremotolerant.

Taxonomy[]

TDPs are found in the clade Tardigrada and more specifically, the branch called Parachela.[1]

Function[]

TDPs are a type of IDP. This means that they have no specific shape unlike traditional folded proteins. There are three families of TDPs. They are each named after where the protein is localized within a cell. These proteins are similar to Late Embryogenesis Abundant (LEA) proteins, except for their specificity to tardigrades. The three families do not resemble each other and are found to be expressed or enriched during desiccation. Unlike traditional proteins, IDPs are not found to precipitate out of solution or denature during high heat.[2]

Discovery of the Cytoplasmic and Secreted Abundant Heat Soluble proteins were found when searching for LEA proteins in tardigrades.[3]

Types[]

Cytoplasmic[]

Cytoplasmic Abundant Heat Soluble (CAHS) proteins have been seen to be highly expressed in response to desiccation. The oldest theory in the mechanism of CAHS proteins is the vitrification hypothesis in which when the organism dries, the viscosity within the cell would increase so much that denaturation and membrane fusion in proteins would stop.[4] A second theory is the water replacement theory in which the CAHS proteins replaces water in the proteins, protecting the bonds that would normally be affected by the hydrogen in water.[5]

Secreted[]

Secreted Abundant Heat Soluble (SAHS) proteins have been noted to be similar to fatty acid binding proteins.[6][7] They are often secreted into media and often associated with special extracellular structures.[8]

Mitochondrial[]

Mitochondrial Abundant Heat Soluble (MAHS) proteins are localized in the mitochondria and are responsible for protecting the mitochondria during desiccation.[9] It is thought that the MAHS proteins act to replace water in the membrane of the mitochondria, preventing uneven rehydration and breaking of the membrane.[10]

References[]

  1. ^ Kamilari M, Jørgensen A, Schiøtt M, Møbjerg N (July 2019). "Comparative transcriptomics suggest unique molecular adaptations within tardigrade lineages". BMC Genomics. 20 (1): 607. doi:10.1186/s12864-019-5912-x. PMC 6652013. PMID 31340759.
  2. ^ Uversky VN (October 2003). "A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders". Journal of Biomolecular Structure & Dynamics. 21 (2): 211–34. doi:10.1080/07391102.2003.10506918. PMID 12956606. S2CID 824815.
  3. ^ Yamaguchi A, Tanaka S, Yamaguchi S, Kuwahara H, Takamura C, Imajoh-Ohmi S, et al. (2012-08-28). "Two novel heat-soluble protein families abundantly expressed in an anhydrobiotic tardigrade". PLOS ONE. 7 (8): e44209. Bibcode:2012PLoSO...744209Y. doi:10.1371/journal.pone.0044209. PMC 3429414. PMID 22937162.
  4. ^ Sakurai M, Furuki T, Akao K, Tanaka D, Nakahara Y, Kikawada T, et al. (April 2008). "Vitrification is essential for anhydrobiosis in an African chironomid, Polypedilum vanderplanki". Proceedings of the National Academy of Sciences of the United States of America. 105 (13): 5093–8. Bibcode:2008PNAS..105.5093S. doi:10.1073/pnas.0706197105. PMC 2278217. PMID 18362351.
  5. ^ Crowe LM (March 2002). "Lessons from nature: the role of sugars in anhydrobiosis". Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology. 131 (3): 505–13. doi:10.1016/S1095-6433(01)00503-7. PMID 11867276.
  6. ^ Fukuda Y, Miura Y, Mizohata E, Inoue T (August 2017). "Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus". FEBS Letters. 591 (16): 2458–2469. doi:10.1002/1873-3468.12752. PMID 28703282. S2CID 3434502.
  7. ^ Fukuda Y, Inoue T (May 2018). "Crystal structure of secretory abundant heat soluble protein 4 from one of the toughest "water bears" micro-animals Ramazzottius Varieornatus". Protein Science. 27 (5): 993–999. doi:10.1002/pro.3393. PMC 5916119. PMID 29493034.
  8. ^ Richaud M, Le Goff E, Cazevielle C, Ono F, Mori Y, Saini NL, et al. (March 2020). "Ultrastructural analysis of the dehydrated tardigrade Hypsibius exemplaris unveils an anhydrobiotic-specific architecture". Scientific Reports. 10 (1): 4324. Bibcode:2020NatSR..10.4324R. doi:10.1038/s41598-020-61165-1. PMC 7062702. PMID 32152342.
  9. ^ Tanaka S, Tanaka J, Miwa Y, Horikawa DD, Katayama T, Arakawa K, et al. (2015-02-12). "Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic Tardigrade improve osmotic tolerance of human cells". PLOS ONE. 10 (2): e0118272. Bibcode:2015PLoSO..1018272T. doi:10.1371/journal.pone.0118272. PMC 4326354. PMID 25675104.
  10. ^ Popova AV, Hundertmark M, Seckler R, Hincha DK (July 2011). "Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1808 (7): 1879–87. doi:10.1016/j.bbamem.2011.03.009. PMID 21443857.
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