Thermostable proteins in the diapausing eggs of Brachionus manjavacas (Rotifera)

Jones, Brande L.; Schneider, Dana; Snell, Terry W.

doi:10.1016/j.cbpa.2012.02.020

Cited by 10 publications

(4 citation statements)

References 55 publications

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“…Likewise, the occurrence of a small heat shock protein with chaperone activity, the antoxidant ferritin and LEA proteins were identified in resting eggs of the monogonont rotifer Brachionus plicatilis 67 . In the related species Brachionus manjavacas, a vitellogenin-like protein and four specific families of heat shock proteins (hsp40, hsp60 and hsp70) also seem to be important for thermotolerance 68,69 . Rather different is the condition found in bdelloid rotifers, as trehalose seems to be absent in these organisms, which lack trehalose biosynthesis genes 70,71 .…”

Section: Discussionmentioning

confidence: 99%

Thermotolerance experiments on active and desiccated states of Ramazzottius varieornatus emphasize that tardigrades are sensitive to high temperatures

Neves

Hvidepil

Sørensen-Hygum

et al. 2020

Sci Rep

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Global warming is already having harmful effects on habitats worldwide and it is therefore important to gain an understanding of how rising temperatures may affect extant animals. Here, we investigate the tolerance to high temperatures of Ramazzottius varieornatus, a tardigrade frequently found in transient freshwater habitats. Using logistic modelling on activity we evaluate the effect of 24 hour temperature exposures on active tardigrades, with or without a short acclimation period, compared to exposures of desiccated tardigrades. We estimate that the 50% mortality temperature for non-acclimated active tardigrades is 37.1 °C, with a small but significant increase to 37.6 °C following acclimation. Desiccated specimens tolerate much higher temperatures, with an estimated 50% mortality temperature of 82.7 °C following 1 hour exposures, but with a significant decrease to 63.1 °C following 24 hour exposures. our results show that metabolically active tardigrades are vulnerable to high temperatures, yet acclimatization could provide a tolerance increase. Desiccated specimens show a much higher resilience-exposure-time is, however, a limiting factor giving tardigrades a restricted window of high temperature tolerance. tardigrades are renowned for their ability to tolerate extreme conditions, but their endurance towards high temperatures clearly has an upper limit-high temperatures thus seem to be their Achilles heel.

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Section: Discussionmentioning

confidence: 99%

Thermotolerance experiments on active and desiccated states of Ramazzottius varieornatus emphasize that tardigrades are sensitive to high temperatures

Neves

Hvidepil

Sørensen-Hygum

et al. 2020

Sci Rep

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“…Recent search for thermostable proteins from monogonont rotifer, Brachionus manjavacas , identified a LEA protein and vitellogenin as major heat soluble proteins in diapausing eggs of the rotifer, but no CAHS/SAHS proteins were found in the search [32] . CAHS and SAHS proteins were conserved among tardigrades, but were not found in other phyla, suggesting that tardigrades might have evolved novel heat-soluble proteins different from LEA proteins as major heat-soluble proteins.…”

Section: Discussionmentioning

confidence: 99%

Two Novel Heat-Soluble Protein Families Abundantly Expressed in an Anhydrobiotic Tardigrade

et al. 2012

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Tardigrades are able to tolerate almost complete dehydration by reversibly switching to an ametabolic state. This ability is called anhydrobiosis. In the anhydrobiotic state, tardigrades can withstand various extreme environments including space, but their molecular basis remains largely unknown. Late embryogenesis abundant (LEA) proteins are heat-soluble proteins and can prevent protein-aggregation in dehydrated conditions in other anhydrobiotic organisms, but their relevance to tardigrade anhydrobiosis is not clarified. In this study, we focused on the heat-soluble property characteristic of LEA proteins and conducted heat-soluble proteomics using an anhydrobiotic tardigrade. Our heat-soluble proteomics identified five abundant heat-soluble proteins. All of them showed no sequence similarity with LEA proteins and formed two novel protein families with distinct subcellular localizations. We named them Cytoplasmic Abundant Heat Soluble (CAHS) and Secretory Abundant Heat Soluble (SAHS) protein families, according to their localization. Both protein families were conserved among tardigrades, but not found in other phyla. Although CAHS protein was intrinsically unstructured and SAHS protein was rich in β-structure in the hydrated condition, proteins in both families changed their conformation to an α-helical structure in water-deficient conditions as LEA proteins do. Two conserved repeats of 19-mer motifs in CAHS proteins were capable to form amphiphilic stripes in α-helices, suggesting their roles as molecular shield in water-deficient condition, though charge distribution pattern in α-helices were different between CAHS and LEA proteins. Tardigrades might have evolved novel protein families with a heat-soluble property and this study revealed a novel repertoire of major heat-soluble proteins in these anhydrobiotic animals.

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“…2009). Several adaptations have been suggested to explain the capability of organisms to survive environmental stresses, particularly trehalose, sucrose, yolk proteins and LEA proteins (Crowe et al, 1998;Hoekstra et al, 2001;Boschetti et al, 2011;Hand et al, 2011;Jones et al, 2012). Although the precise function of SGs in the physiology of rotifers is yet to be understood, their formation is most probably related to survival during periods of stress.…”

Section: Discussionmentioning

confidence: 98%

“…The stressors are (1) osmotic stress, (2) heat stress or (3) nutrient deprivation. Rotifers were judged dead by immobility and lack of any ciliary or internal movements for 3 s of observation as consistent with the other studies (Snell et al, 1991;Jones et al, 2012). Twenty technical replicates were used for each of the stressors, and all survival experiments were conducted with six biological replicates.…”

Section: Assessing Survival Of Neonates During Periods Of Environmentmentioning

confidence: 98%

Stress granules form in Brachionus manjavacas (Rotifera) in response to a variety of stressors

Jones

VanLoozen

Kim

et al. 2013

Comparative Biochemistry and Physiology Part A: Molecular &

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Thermostable proteins in the diapausing eggs of Brachionus manjavacas (Rotifera)

Cited by 10 publications

References 55 publications

Thermotolerance experiments on active and desiccated states of Ramazzottius varieornatus emphasize that tardigrades are sensitive to high temperatures

Thermotolerance experiments on active and desiccated states of Ramazzottius varieornatus emphasize that tardigrades are sensitive to high temperatures

Two Novel Heat-Soluble Protein Families Abundantly Expressed in an Anhydrobiotic Tardigrade

Stress granules form in Brachionus manjavacas (Rotifera) in response to a variety of stressors

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