分子科学研究所

Site Search

News

News Detail

2021/11/04

Press Release

Gather before dry up! Tardigrade protein self-assembles into fibrous condensates under desiccation condition

Collaborative research groups in Japan have explored the molecular mechanisms of desiccation tolerance in tardigrades. They have visualized spontaneous assembling of tardigrade’s cytosolic abundant heat-soluble proteins into fibrous condensates under desiccation-mimicking conditions, illustrating an adaptation strategy of organisms to extreme environments.

-----------------------------------------------------------------------------------------------

Tardigrades, also known as water bears or moss piglets, are unique microscopic animals that enter cryptobiotic states upon desiccation and thereby survive in extreme conditions, including radiation, air deprivation, and even exposure to space vacuum. Therefore, tardigrades have attracted the attention of many researchers attempting to unravel their cryptobiotic mechanisms, which remain mostly elusive. The collaborative groups in Japan, including researchers at Exploratory Research Center on Life and Living Systems (ExCELLS) of National Institutes of Natural Sciences, observed changes in molecular behaviors of a heat-soluble protein abundant in tardigrade cytosols (called CAHS1 protein). Their integrative spectroscopic and microscopic data demonstrate that the protein self-assembles into fibrous condensates under desiccation-mimicking conditions in a reversible manner. This dynamic protein organization suggests multistep anhydrobiotic mechanisms, including the reversible formation of protective compartments for desiccation-sensitive biomolecules, water-holding gelation, and maintenance of the integrity of biomolecular complexes under extremely dry conditions. These findings illustrate an adaptation strategy of organisms to extreme environments without water.

Spontaneous assembling of CAHS1 proteins into fibrous condensates
under desiccation-mimicking conditions

High-speed atomic force microscopy imaging of fibril formation (left) and fluorescence imaging of reversible condensation (right) of the CAHS1 proteins derived from Ramazzottius varieornatus.

 

Information of the paper

Authors: 
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 and Koichi Kato

Journal Name: Scientific Reports

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

DOI:10.1038/s41598-021-00724-6

 

Contact

Koichi KATO
Exploratory Research Center on Life and Living Systems (ExCELLS)
Institute for Molecular Science (IMS)
Natural Institutes of Natural Sciences, Okazaki.
TEL: +81-564-59-5225
E-mail: kkato_at_excells.orion.ac.jp
(Please replace the “_at_” with @)

 

Press contact

Exploratory Research Center on Life and Living Systems (ExCELLS)
Natural Institutes of Natural Sciences, Okazaki.
TEL: +81-564-59-5201 FAX: +81-564-59-5202
E-mail: press_at_excells.orion.ac.jp
(Please replace the “_at_” with @)