Cargando…

Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade

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 extremotolera...

Descripción completa

Detalles Bibliográficos
Autores principales: Yagi-Utsumi, Maho, Aoki, Kazuhiro, Watanabe, Hiroki, Song, Chihong, Nishimura, Seiji, Satoh, Tadashi, Yanaka, Saeko, Ganser, Christian, Tanaka, Sae, Schnapka, Vincent, Goh, Ean Wai, Furutani, Yuji, Murata, Kazuyoshi, Uchihashi, Takayuki, Arakawa, Kazuharu, Kato, Koichi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8569203/
https://www.ncbi.nlm.nih.gov/pubmed/34737320
http://dx.doi.org/10.1038/s41598-021-00724-6
_version_ 1784594602516283392
author Yagi-Utsumi, Maho
Aoki, Kazuhiro
Watanabe, Hiroki
Song, Chihong
Nishimura, Seiji
Satoh, Tadashi
Yanaka, Saeko
Ganser, Christian
Tanaka, Sae
Schnapka, Vincent
Goh, Ean Wai
Furutani, Yuji
Murata, Kazuyoshi
Uchihashi, Takayuki
Arakawa, Kazuharu
Kato, Koichi
author_facet Yagi-Utsumi, Maho
Aoki, Kazuhiro
Watanabe, Hiroki
Song, Chihong
Nishimura, Seiji
Satoh, Tadashi
Yanaka, Saeko
Ganser, Christian
Tanaka, Sae
Schnapka, Vincent
Goh, Ean Wai
Furutani, Yuji
Murata, Kazuyoshi
Uchihashi, Takayuki
Arakawa, Kazuharu
Kato, Koichi
author_sort Yagi-Utsumi, Maho
collection PubMed
description 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 Online
Article
Text
id pubmed-8569203
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-85692032021-11-05 Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade Yagi-Utsumi, Maho Aoki, Kazuhiro Watanabe, Hiroki Song, Chihong Nishimura, Seiji Satoh, Tadashi Yanaka, Saeko Ganser, Christian Tanaka, Sae Schnapka, Vincent Goh, Ean Wai Furutani, Yuji Murata, Kazuyoshi Uchihashi, Takayuki Arakawa, Kazuharu Kato, Koichi Sci Rep Article 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. Nature Publishing Group UK 2021-11-04 /pmc/articles/PMC8569203/ /pubmed/34737320 http://dx.doi.org/10.1038/s41598-021-00724-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Yagi-Utsumi, Maho
Aoki, Kazuhiro
Watanabe, Hiroki
Song, Chihong
Nishimura, Seiji
Satoh, Tadashi
Yanaka, Saeko
Ganser, Christian
Tanaka, Sae
Schnapka, Vincent
Goh, Ean Wai
Furutani, Yuji
Murata, Kazuyoshi
Uchihashi, Takayuki
Arakawa, Kazuharu
Kato, Koichi
Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade
title 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_short Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade
title_sort desiccation-induced fibrous condensation of cahs protein from an anhydrobiotic tardigrade
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8569203/
https://www.ncbi.nlm.nih.gov/pubmed/34737320
http://dx.doi.org/10.1038/s41598-021-00724-6
work_keys_str_mv AT yagiutsumimaho desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT aokikazuhiro desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT watanabehiroki desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT songchihong desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT nishimuraseiji desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT satohtadashi desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT yanakasaeko desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT ganserchristian desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT tanakasae desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT schnapkavincent desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT goheanwai desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT furutaniyuji desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT muratakazuyoshi desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT uchihashitakayuki desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT arakawakazuharu desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade
AT katokoichi desiccationinducedfibrouscondensationofcahsproteinfromananhydrobiotictardigrade