JOURNAL ARTICLE
Tardigrade proteins: molecular tools in the phenomenon of anhydrobiosis.
Published In: Zoological Journal of the Linnean Society, 2024, v. 200, n. 1. P. 269 1 of 3
Database: Academic Search Ultimate 2 of 3
Authored By: Krakowiak, Michalina; Bartylak, Tomasz; Kmita, Hanna; Kaczmarek, Łukasz; Nawrot, Robert 3 of 3
Abstract
This article reviews the proteins involved in anhydrobiosis, a desiccation survival strategy in tardigrades (water bears), focusing on their roles in protecting cellular structures, macromolecules, and DNA during extreme dehydration. Key protein groups include tardigrade-specific intrinsically disordered proteins (TDPs) such as cytoplasmic abundant heat soluble (CAHS), mitochondrial abundant heat soluble (MAHS), secretory abundant heat soluble (SAHS), and damage suppressor (Dsup), as well as heat shock proteins (Hsps) and reactive oxygen species-eliminating enzymes (ROS-E). The review highlights the diverse molecular functions of these proteins, including stabilization of proteins and membranes, elimination of oxidative damage, and DNA protection, while noting that the precise mechanisms and contributions of many proteins remain incompletely understood. It also discusses species-specific variations in protein expression and the potential synergistic roles of trehalose and other bioprotectants in tardigrade desiccation tolerance.
Additional Information
- Source:Zoological Journal of the Linnean Society. 2024/01, Vol. 200, Issue 1, p269
- Document Type:Article
- Subject Area:Zoology
- Publication Date:2024
- ISSN:0024-4082
- DOI:10.1093/zoolinnean/zlad066
- Accession Number:174559767
- Copyright Statement:Copyright of Zoological Journal of the Linnean Society is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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