Tardigrade Secretory-Abundant Heat-Soluble Protein Varies Entrance Propensity Depending on the Amino-Acid Sequence

Miyazawa, Kazuhisa; Itoh, Satoru; Yoshida, Yuki; Arakawa, Kazuharu; Okumura, Hisashi

doi:10.1021/acs.jpcb.1c10788

Cited by 3 publications

(1 citation statement)

References 35 publications

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“…While many desiccation‐related IDPs have been shown to possess transient helicity, which increases upon drying, this is by no means an absolute rule. For example, SAHS proteins from tardigrades contain more stable beta‐structure (Fukuda et al, 2017; Fukuda & Inoue, 2018; Miyazawa et al, 2021; Miyazawa et al, 2022), as do some LEA proteins (Furuki & Sakurai, 2014). Even CAHS proteins are known to contain transient beta‐structure, albeit localized to their terminal regions (Eicher et al, 2022; Sanchez‐Martinez, Nguyen, et al, 2023).…”

Section: Discussionmentioning

confidence: 99%

Helicity of a tardigrade disordered protein contributes to its protective function during desiccation

Biswas,

Gollub,

et al. 2024

Protein Science

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In order to survive extreme drying (anhydrobiosis), many organisms, spanning every kingdom of life, accumulate intrinsically disordered proteins (IDPs). For decades, the ability of anhydrobiosis‐related IDPs to form transient amphipathic helices has been suggested to be important for promoting desiccation tolerance. However, evidence empirically supporting the necessity and/or sufficiency of helicity in mediating anhydrobiosis is lacking. Here we demonstrate that the linker region of CAHS D, a desiccation‐related IDP from the tardigrade Hypsibius exemplaris, that contains significant helical structure, is the protective portion of this protein. Perturbing the sequence composition and grammar of the linker region of CAHS D, through the insertion of helix‐breaking prolines, modulating the identity of charged residues, or replacement of hydrophobic amino acids with serine or glycine residues results in variants with different degrees of helical structure. Importantly, correlation of protective capacity and helical content in variants generated through different helix perturbing modalities do not show as strong a trend, suggesting that while helicity is important it is not the only property that makes a protein protective during desiccation. These results provide direct evidence for the decades old theory that helicity of desiccation‐related IDPs is linked to their anhydrobiotic capacity.This article is protected by copyright. All rights reserved.

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Section: Discussionmentioning

confidence: 99%

Helicity of a tardigrade disordered protein contributes to its protective function during desiccation

Biswas,

Gollub,

et al. 2024

Protein Science

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The Evolution of Temperature and Desiccation-Related Protein Families in Tardigrada Reveals a Complex Acquisition of Extremotolerance

Fleming,

Pisani,

Arakawa

2023

Genome Biology and Evolution

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Tardigrada is an ecdysozoan lineage most famous for its resilience. Tardigrades can tolerate high doses of radiation, low oxygen environments, desiccation and both high and low temperatures under a dormant state called anhydrobiosis, which is a reversible halt of metabolism upon almost complete desiccation. A large amount of research has focused on the genetic pathways related to these capabilities, and a number of genes have been identified and linked to tardigrade’s extremotolerant response. However, the history of these genes is unclear, and the origins and history of extremotolerant genes within Tardigrada remain a mystery. Here, we generate the first phylogenies of six separate gene families linked with desiccation and radiation tolerance in Tardigrada: Cytosolic Abundant Heat Soluble Protein (CAHS), Mitochondrial Abundant Heat Soluble Protein (MAHS), Secretory Abundant Heat Soluble Protein (SAHS), Meiotic Recombination 11 Homolog (MRE11) and the newly discovered Echiniscus testudo Abundant Heat Soluble Proteins (EtAHS Alpha and Beta). Our study of the gene duplications suggests a link between the evolution of these genes and aquatic to limno-terrestrial transitions within tardigrades. Our results suggest that tardigrades likely transitioned from the marine to limno-terrestrial environment only twice, once in stem-Eutardigrada and once in Heterotardigrada, which explains the unique adaptations to anhydrobiosis present in both classes.

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Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation

Okumura

Itoh

2022

Molecules

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Alzheimer’s disease is understood to be caused by amyloid fibrils and oligomers formed by aggregated amyloid-β (Aβ) peptides. This review article presents molecular dynamics (MD) simulation studies of Aβ peptides and Aβ fragments on their aggregation, aggregation inhibition, amyloid fibril conformations in equilibrium, and disruption of the amyloid fibril by ultrasonic wave and infrared laser irradiation. In the aggregation of Aβ, a β-hairpin structure promotes the formation of intermolecular β-sheet structures. Aβ peptides tend to exist at hydrophilic/hydrophobic interfaces and form more β-hairpin structures than in bulk water. These facts are the reasons why the aggregation is accelerated at the interface. We also explain how polyphenols, which are attracting attention as aggregation inhibitors of Aβ peptides, interact with Aβ. An MD simulation study of the Aβ amyloid fibrils in equilibrium is also presented: the Aβ amyloid fibril has a different structure at one end from that at the other end. The amyloid fibrils can be destroyed by ultrasonic wave and infrared laser irradiation. The molecular mechanisms of these amyloid fibril disruptions are also explained, particularly focusing on the function of water molecules. Finally, we discuss the prospects for developing treatments for Alzheimer’s disease using MD simulations.

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Tardigrade Secretory-Abundant Heat-Soluble Protein Varies Entrance Propensity Depending on the Amino-Acid Sequence

Cited by 3 publications

References 35 publications

Helicity of a tardigrade disordered protein contributes to its protective function during desiccation

Helicity of a tardigrade disordered protein contributes to its protective function during desiccation

The Evolution of Temperature and Desiccation-Related Protein Families in Tardigrada Reveals a Complex Acquisition of Extremotolerance

Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation

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