Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade
Abstract Anhydrobiosis, one of the most extensively studied forms of cryptobiosis, is induced in certain organisms as a response to desiccation. Anhydrobiotic species has been hypothesized to produce substances that can protect their biological components and/or cell membranes without water. In extr...
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Nature Portfolio
2021
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oai:doaj.org-article:bd8100bd830e4050bb9c5f0ddb3109b92021-11-08T10:52:24ZDesiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade10.1038/s41598-021-00724-62045-2322https://doaj.org/article/bd8100bd830e4050bb9c5f0ddb3109b92021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-00724-6https://doaj.org/toc/2045-2322Abstract Anhydrobiosis, one of the most extensively studied forms of cryptobiosis, is induced in certain organisms as a response to desiccation. Anhydrobiotic species has been hypothesized to produce substances that can protect their biological components and/or cell membranes without water. In extremotolerant tardigrades, highly hydrophilic and heat-soluble protein families, cytosolic abundant heat-soluble (CAHS) proteins, have been identified, which are postulated to be integral parts of the tardigrades’ response to desiccation. In this study, to elucidate these protein functions, we performed in vitro and in vivo characterizations of the reversible self-assembling property of CAHS1 protein, a major isoform of CAHS proteins from Ramazzottius varieornatus, using a series of spectroscopic and microscopic techniques. We found that CAHS1 proteins homo-oligomerized via the C-terminal α-helical region and formed a hydrogel as their concentration increased. We also demonstrated that the overexpressed CAHS1 proteins formed condensates under desiccation-mimicking conditions. These data strongly suggested that, upon drying, the CAHS1 proteins form oligomers and eventually underwent sol–gel transition in tardigrade cytosols. Thus, it is proposed that the CAHS1 proteins form the cytosolic fibrous condensates, which presumably have variable mechanisms for the desiccation tolerance of tardigrades. These findings provide insights into molecular strategies of organisms to adapt to extreme environments.Maho Yagi-UtsumiKazuhiro AokiHiroki WatanabeChihong SongSeiji NishimuraTadashi SatohSaeko YanakaChristian GanserSae TanakaVincent SchnapkaEan Wai GohYuji FurutaniKazuyoshi MurataTakayuki UchihashiKazuharu ArakawaKoichi KatoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021) |
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Medicine R Science Q Maho Yagi-Utsumi Kazuhiro Aoki Hiroki Watanabe Chihong Song Seiji Nishimura Tadashi Satoh Saeko Yanaka Christian Ganser Sae Tanaka Vincent Schnapka Ean Wai Goh Yuji Furutani Kazuyoshi Murata Takayuki Uchihashi Kazuharu Arakawa Koichi Kato Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade |
| description |
Abstract Anhydrobiosis, one of the most extensively studied forms of cryptobiosis, is induced in certain organisms as a response to desiccation. Anhydrobiotic species has been hypothesized to produce substances that can protect their biological components and/or cell membranes without water. In extremotolerant tardigrades, highly hydrophilic and heat-soluble protein families, cytosolic abundant heat-soluble (CAHS) proteins, have been identified, which are postulated to be integral parts of the tardigrades’ response to desiccation. In this study, to elucidate these protein functions, we performed in vitro and in vivo characterizations of the reversible self-assembling property of CAHS1 protein, a major isoform of CAHS proteins from Ramazzottius varieornatus, using a series of spectroscopic and microscopic techniques. We found that CAHS1 proteins homo-oligomerized via the C-terminal α-helical region and formed a hydrogel as their concentration increased. We also demonstrated that the overexpressed CAHS1 proteins formed condensates under desiccation-mimicking conditions. These data strongly suggested that, upon drying, the CAHS1 proteins form oligomers and eventually underwent sol–gel transition in tardigrade cytosols. Thus, it is proposed that the CAHS1 proteins form the cytosolic fibrous condensates, which presumably have variable mechanisms for the desiccation tolerance of tardigrades. These findings provide insights into molecular strategies of organisms to adapt to extreme environments. |
| format |
article |
| author |
Maho Yagi-Utsumi Kazuhiro Aoki Hiroki Watanabe Chihong Song Seiji Nishimura Tadashi Satoh Saeko Yanaka Christian Ganser Sae Tanaka Vincent Schnapka Ean Wai Goh Yuji Furutani Kazuyoshi Murata Takayuki Uchihashi Kazuharu Arakawa Koichi Kato |
| author_facet |
Maho Yagi-Utsumi Kazuhiro Aoki Hiroki Watanabe Chihong Song Seiji Nishimura Tadashi Satoh Saeko Yanaka Christian Ganser Sae Tanaka Vincent Schnapka Ean Wai Goh Yuji Furutani Kazuyoshi Murata Takayuki Uchihashi Kazuharu Arakawa Koichi Kato |
| author_sort |
Maho Yagi-Utsumi |
| title |
Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade |
| title_short |
Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade |
| title_full |
Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade |
| title_fullStr |
Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade |
| title_full_unstemmed |
Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade |
| title_sort |
desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade |
| publisher |
Nature Portfolio |
| publishDate |
2021 |
| url |
https://doaj.org/article/bd8100bd830e4050bb9c5f0ddb3109b9 |
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1718442563263791104 |