The biology of tardigrade disordered proteins in extreme stress tolerance

Abstract Disordered proteins have long been known to help mediate tolerance to different abiotic stresses including freezing, osmotic stress, high temperatures, and desiccation in a diverse set of organisms. Recently, three novel families of intrinsically disordered proteins were identified in tardi...

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Main Authors: Cherie Hesgrove, Thomas C. Boothby
Format: Article
Language:English
Published: BMC 2020-11-01
Series:Cell Communication and Signaling
Subjects:
Online Access:http://link.springer.com/article/10.1186/s12964-020-00670-2
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spelling doaj-22af78abf11f490391ed9222d6612d472020-11-25T04:08:37ZengBMCCell Communication and Signaling1478-811X2020-11-0118111510.1186/s12964-020-00670-2The biology of tardigrade disordered proteins in extreme stress toleranceCherie Hesgrove0Thomas C. Boothby1Department of Molecular Biology, University of WyomingDepartment of Molecular Biology, University of WyomingAbstract Disordered proteins have long been known to help mediate tolerance to different abiotic stresses including freezing, osmotic stress, high temperatures, and desiccation in a diverse set of organisms. Recently, three novel families of intrinsically disordered proteins were identified in tardigrades, microscopic animals capable of surviving a battery of environmental extremes. These three families include the Cytoplasmic-, Secreted-, and Mitochondrial- Abundant Heat Soluble (CAHS, SAHS, and MAHS) proteins, which are collectively termed Tardigrade Disordered Proteins (TDPs). At the level of sequence conservation TDPs are unique to tardigrades, and beyond their high degree of disorder the CAHS, SAHS, and MAHS families do not resemble one another. All three families are either highly expressed constitutively, or significantly enriched in response to desiccation. In vivo, ex vivo, and in vitro experiments indicate functional roles for members of each TDP family in mitigating cellular perturbations induced by various abiotic stresses. What is currently lacking is a comprehensive and holistic understanding of the fundamental mechanisms by which TDPs function, and the properties of TDPs that allow them to function via those mechanisms. A quantitative and systematic approach is needed to identify precisely what cellular damage TDPs work to prevent, what sequence features are important for these functions, and how those sequence features contribute to the underlying mechanisms of protection. Such an approach will inform us not only about these fascinating proteins, but will also provide insights into how the sequence of a disordered protein can dictate its functional, structural, and dynamic properties. Video Abstract Graphical abstracthttp://link.springer.com/article/10.1186/s12964-020-00670-2TardigradeIntrinsically disordered proteinsTardigrade disordered proteinCytoplasmic abundant heat soluble proteinSecreted abundant heat soluble proteinMitochondrial abundant heat soluble protein
collection DOAJ
language English
format Article
sources DOAJ
author Cherie Hesgrove
Thomas C. Boothby
spellingShingle Cherie Hesgrove
Thomas C. Boothby
The biology of tardigrade disordered proteins in extreme stress tolerance
Cell Communication and Signaling
Tardigrade
Intrinsically disordered proteins
Tardigrade disordered protein
Cytoplasmic abundant heat soluble protein
Secreted abundant heat soluble protein
Mitochondrial abundant heat soluble protein
author_facet Cherie Hesgrove
Thomas C. Boothby
author_sort Cherie Hesgrove
title The biology of tardigrade disordered proteins in extreme stress tolerance
title_short The biology of tardigrade disordered proteins in extreme stress tolerance
title_full The biology of tardigrade disordered proteins in extreme stress tolerance
title_fullStr The biology of tardigrade disordered proteins in extreme stress tolerance
title_full_unstemmed The biology of tardigrade disordered proteins in extreme stress tolerance
title_sort biology of tardigrade disordered proteins in extreme stress tolerance
publisher BMC
series Cell Communication and Signaling
issn 1478-811X
publishDate 2020-11-01
description Abstract Disordered proteins have long been known to help mediate tolerance to different abiotic stresses including freezing, osmotic stress, high temperatures, and desiccation in a diverse set of organisms. Recently, three novel families of intrinsically disordered proteins were identified in tardigrades, microscopic animals capable of surviving a battery of environmental extremes. These three families include the Cytoplasmic-, Secreted-, and Mitochondrial- Abundant Heat Soluble (CAHS, SAHS, and MAHS) proteins, which are collectively termed Tardigrade Disordered Proteins (TDPs). At the level of sequence conservation TDPs are unique to tardigrades, and beyond their high degree of disorder the CAHS, SAHS, and MAHS families do not resemble one another. All three families are either highly expressed constitutively, or significantly enriched in response to desiccation. In vivo, ex vivo, and in vitro experiments indicate functional roles for members of each TDP family in mitigating cellular perturbations induced by various abiotic stresses. What is currently lacking is a comprehensive and holistic understanding of the fundamental mechanisms by which TDPs function, and the properties of TDPs that allow them to function via those mechanisms. A quantitative and systematic approach is needed to identify precisely what cellular damage TDPs work to prevent, what sequence features are important for these functions, and how those sequence features contribute to the underlying mechanisms of protection. Such an approach will inform us not only about these fascinating proteins, but will also provide insights into how the sequence of a disordered protein can dictate its functional, structural, and dynamic properties. Video Abstract Graphical abstract
topic Tardigrade
Intrinsically disordered proteins
Tardigrade disordered protein
Cytoplasmic abundant heat soluble protein
Secreted abundant heat soluble protein
Mitochondrial abundant heat soluble protein
url http://link.springer.com/article/10.1186/s12964-020-00670-2
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