Crystal structure of secretory abundant heat soluble protein 4 from one of the toughest “water bears” micro‐animals <i>Ramazzottius Varieornatus</i>

Fukuda, Youichi; Inoue, Tsuyoshi

doi:10.1002/pro.3393

Cited by 18 publications

(26 citation statements)

References 37 publications

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“…TDPs appear to be unique to tardigrades, with most possessing no sequence homology to non-tardigrade genes, proteins, or conserved domains [ 7 , 24 , 25 ]. There are a few exceptions, such as SAHS proteins which show low sequence homology to the Fatty Acid Binding Protein (FABP) family [ 32 , 33 ]. The low homology to FABPs seen for some SAHS proteins mirrors the lower predicted disorder for the SAHS family relative to other TDPs [ 7 ].…”

Section: Main Textmentioning

confidence: 99%

“…A series of crystallographic studies on the SAHS proteins in Ramazzottius varieornatus have revealed the similarity between some SAHS proteins and a versatile class of proteins called fatty acid binding proteins (FABPs). The structures of Rv SAHS1 [ 33 ] and Rv SAHS4 [ 32 ] are similar to other canonical FABPs, characterized by an antiparallel β-barrel with an internal FA binding pocket, and a helix-turn-helix lid. In their 2017 study, Fukuda et al found that Rv SAHS1 binds to small fatty acids, but that bulky residues present in its two ligand binding sites (LBS1 and LBS2) prevent this protein from binding large membrane phospholipids.…”

Section: Main Textmentioning

confidence: 99%

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The biology of tardigrade disordered proteins in extreme stress tolerance

Hesgrove

Boothby

2020

Cell Commun Signal

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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. Graphical abstract

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Section: Main Textmentioning

confidence: 99%

Section: Main Textmentioning

confidence: 99%

The biology of tardigrade disordered proteins in extreme stress tolerance

Hesgrove

Boothby

2020

Cell Commun Signal

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“…While many tardigrade‐specific proteins with low or no sequence similarities to well‐characterized proteins are found, structural biology has revealed that some of their three‐dimensional structures are unexpectedly quite similar to those of known proteins. For example, secretory abundant heat soluble (SAHS) proteins are only found in some anhydrobiotic tardigrades, 27 but their structures are almost the same as those of fatty acid binding proteins (FABPs) and SAHS proteins can bind to fatty acids and other hydrophobic compounds as FABPs do 28,29 . We here showed that the TC2P is another example for “much different primary structure but the same tertiary structure.” More structural and functional analyses on tardigrade proteins may answer to why tardigrade proteins have evolved in such a unique way.…”

Section: Resultsmentioning

confidence: 75%

Structural insights into a C2 domain protein specifically found in tardigrades

Fukuda

Inoue

2020

Protein Science

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Some tardigrades can survive extremely desiccated conditions through transition into a state called anhydrobiosis. Anhydrobiotic tardigrades have proteins unique to them and they are thought to be keys to the understanding of unusual desiccation resistance. In fact, previous transcriptome data show that several tardigrade‐specific proteins are significantly upregulated under desiccated conditions. However, their physiological roles and chemical properties have been ambiguous because they show low or no similarity of amino acid sequences to proteins found in other organisms. Here, we report a crystal structure of one of such proteins. This protein shows a β‐sandwich structure composed of 8 β‐strands, three Ca2+‐binding sites, and hydrophobic residues on Ca2+‐binding (CBD) loops, which resemble characteristics of C2 domain proteins. We therefore conveniently describe this protein as tardigrade C2 domain protein (TC2P). Because the C2 domain functions as a Ca2+‐mediated membrane docking module, which is related to signal transduction or membrane trafficking, TC2Ps may play a role in Ca2+‐triggered phenomenon under desiccated situations. Our finding provides not only structural insights into a newly discovered desiccation‐related protein family but also insights into the evolution and diversity of C2 domain proteins.

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“…The main result of the study (result 1) shows that TDPs can protect E. coli BL21 under conditions of lyophilization [19,35] , allowing the storage of engineered strains at room temperature. A possible explanation for this effect was postulated in the waterreplacement hypothesis proposed by Thomas C. Boothby et al, according to which the TDPs are able to replace the hydrogen bonds formed between water and the cellular macromolecules.…”

Section: Discussionmentioning

confidence: 98%

Room-temperature Storage of Lyophilized Engineered Bacteria using Tardigrade Intrinsically Disordered Proteins

Yang

Jiao

Zhang

et al. 2021

Preprint

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Tardigrades, which live in transiently wet environments such as moss, are well-known for their extreme resistance to desiccation. Tardigrade intrinsically disordered proteins (TDPs) have been reported to also protect bacteria and yeast under desiccation. In this study, we utilized lyophilization to achieve room-temperature storage of engineered bacteria. By using TDPs, engineered bacteria are protected under lyophilization and their original functions are preserved. This study shows that TDPs can be expressed in the Escherichia coli (E. coli) BL21 and DH5α, and bacteria treated with Cytosolic-abundant heat soluble protein (CAHS) 106094 displayed the highest survival rate after lyophilization. Moreover, this study shows that the co-expression of TDPs can improve the preservation of bacteria and maintain high survival rates after prolonged room temperature storage. Additionally, the TDPs can be expressed using different vectors, which means that they can be used in different types of engineered bacteria. This study offers a new storage method that not only improves the storage of biological material for industrial and daily usage, but also for future iGEM (International Genetically Engineered Machine Competition) teams to store and use their engineered bacteria in different applications.

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Crystal structure of secretory abundant heat soluble protein 4 from one of the toughest “water bears” micro‐animals Ramazzottius Varieornatus

Cited by 18 publications

References 37 publications

The biology of tardigrade disordered proteins in extreme stress tolerance

The biology of tardigrade disordered proteins in extreme stress tolerance

Structural insights into a C2 domain protein specifically found in tardigrades

Room-temperature Storage of Lyophilized Engineered Bacteria using Tardigrade Intrinsically Disordered Proteins

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