Thermal stress induces a distinct transcriptome profile in the Pacific oyster Crassostrea gigas

Lim, Hyun-Jeong; Kim, Bomi; Hwang, In Joon; Lee, Jeong-Soo; Choi, Ik‐Young; Kim, Youn-Jung; Rhee, Jae-Sung

doi:10.1016/j.cbd.2016.06.006

Cited by 34 publications

(31 citation statements)

References 49 publications

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“…Biochemical adaptation of proteins to temperature has been documented for a variety of proteins across a diversity of ectothermic taxa (Tattersall et al, 2012;Fields et al, 2015;Lim et al, 2016). A key factor that underlies these temperature-adaptive differences is the need for an appropriate degree of structural stability at normal cellular temperatures (Somero et al, 2017).…”

Section: Discussion Biochemical Adaptation Mechanisms Of High Thermalmentioning

confidence: 99%

Heat-resistant cytosolic malate dehydrogenases (cMDHs) of thermophilic intertidal snails (genus Echinolittorina): protein underpinnings of tolerance to body temperatures reaching 55°C

Liao

Zhang

et al. 2017

Journal of Experimental Biology

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Snails of the genus Echinolittorina are among the most heat-tolerant animals; they experience average body temperatures near 41-44°C in summer and withstand temperatures up to at least 55°C. Here, we demonstrate that heat stability of function (indexed by the MichaelisMenten constant of the cofactor NADH, K M NADH ) and structure (indexed by rate of denaturation) of cytosolic malate dehydrogenases (cMDHs) of two congeners (E. malaccana and E. radiata) exceeds values previously found for orthologs of this protein from less thermophilic species. The ortholog of E. malaccana is more heat stable than that of E. radiata, in keeping with the congeners' thermal environments. Only two inter-congener differences in amino acid sequence in these 332 residue proteins were identified. In both cases ( positions 48 and 114), a glycine in the E. malaccana ortholog is replaced by a serine in the E. radiata protein. To explore the relationship between structure and function and to characterize how amino acid substitutions alter stability of different regions of the enzyme, we used molecular dynamics simulation methods. These computational methods allow determination of thermal effects on finescale movements of protein components, for example, by estimating the root mean square deviation in atom position over time and the root mean square fluctuation for individual residues. The minor changes in amino acid sequence favor temperature-adaptive change in flexibility of regions in and around the active sites. Interspecific differences in effects of temperature on fine-scale protein movements are consistent with the differences in thermal effects on binding and rates of heat denaturation.

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Section: Discussion Biochemical Adaptation Mechanisms Of High Thermalmentioning

confidence: 99%

Heat-resistant cytosolic malate dehydrogenases (cMDHs) of thermophilic intertidal snails (genus Echinolittorina): protein underpinnings of tolerance to body temperatures reaching 55°C

Liao

Zhang

et al. 2017

Journal of Experimental Biology

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“…Among the many indicators of physiological responses to thermal challenge, the respiration behavior and individual-level metabolic rates (especially oxygen consumption rate) have been widely used to assess the physiological state in response to stress tolerance or adaptation during exposure to heat stress (Sobral & Widdows, 1997;Saucedo et al, 2004;Sarà et al, 2008;Dowd & Somero, 2013;Frisk, Steffensen & Skov, 2013;Wang et al, 2015;Casas et al, 2018). Successful persistence or tolerance requires molecular adaptations to compensate for the impaired metabolism, triggered by changes of temperature (Lim et al, 2016). Moreover, investigating the correlation between individual-level responses and molecular changes is useful toward a better understanding of the responses and regulating mechanisms from an overall perspective.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, investigating the correlation between individual-level responses and molecular changes is useful toward a better understanding of the responses and regulating mechanisms from an overall perspective. Recently, research has increasingly focused on molecular adaptation or tolerance of marine bivalves to heat stress, and new analytic techniques, such as transcriptomics (Lim et al, 2016;Nie et al, 2017;Yang et al, 2017;Juárez et al, 2018;Zhang et al, 2019) and metabolomics (Ellis et al, 2014;Digilio et al, 2016), were used. The mantle tissue of mollusks has multiple functions, which include ligament secretion and sensorial activities; moreover, this tissue is very responsive to external stimuli (Artigaud et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Metabolic response of Scapharca subcrenata to heat stress using GC/MS-based metabolomics

Jiang

Jiao

Sun

et al. 2020

PeerJ

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Marine mollusks are commonly subjected to heat stress. To evaluate the effects of heat stress on the physiological metabolism of the ark shell Scapharca subcrenata, clams were exposed to different high temperatures (24, 28 and 32 °C) for 72 h. The oxygen consumption and ammonia excretion rates were measured at 2, 12, 24, 48 and 72 h. The results indicated that the metabolic rates of the ark shell significantly increased with increasing heat stress, accompanied by mortalities in response to prolonged exposure. A metabolomics approach based on gas chromatography coupled with mass spectrometry was further applied to assess the changes of metabolites in the mantle of the ark shell at 32 °C. Moreover, multivariate and pathway analyses were conducted for the different metabolites. The results showed that the heat stress caused changes in energy metabolism, amino acid metabolism, osmotic regulation, carbohydrate metabolism and lipid metabolism through different metabolic pathways. These results are consistent with the significant changes of oxygen consumption rate and ammonia excretion rate. The present study contributes to the understanding of the impacts of heat stress on intertidal bivalves and elucidates the relationship between individual-level responses and underlying molecular metabolic dynamics.

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“…Hsp70 chaperones frequently function as assembly factors. Thus, next to an extraordinary capability to adapt to stress conditions (63,64), the large number of Hsp70s may play a crucial role in shell formation. With respect to longevity, the most striking observation from our analyses is the opposing numbers of Hsp90 proteins in N.furzeri and H.glaber.…”

Section: Resultsmentioning

confidence: 99%

Pervasive convergent evolution and extreme phenotypes define chaperone requirements of protein homeostasis

Draceni

Pechmann

2019

Preprint

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Maintaining protein homeostasis is an essential requirement for cell and organismal viability. An elaborate regulatory system within cells, the protein homeostasis network, safeguards that proteins are correctly folded and functional. At the heart of this regulatory system lies a class of specialized protein quality control enzymes called chaperones that are tasked with assisting proteins in their folding, avoiding aggregation, and degradation. Failure and decline of protein homeostasis are directly associated with conditions of aging and aging-related neurodegenerative diseases such as Alzheimer's and Parkinson's. However, it is not clear what tips the balance of protein homeostasis and leads to onset of aging and diseases. Here, we present a comparative genomics analysis of protein homeostasis in eukaryotes and report general principles of maintaining protein homeostasis across the eukaryotic tree of life. Expanding a previous analysis of 16 eukaryotes to 216 eukaryotic genomes, we find a strong correlation between the size of eukaryotic chaperone networks and size of the genomes that is distinct for different species kingdoms. Importantly, organisms with pronounced phenotypes clearly buck this trend.Northobranchius furzeri, the shortest-lived vertebrate and widely used model for fragile protein homeostasis is found to be chaperone limited. Heterocephalus glaber as the longest-lived rodent thus especially robust organism is characterized by above average numbers of chaperones. Our work thus indicates that the balance in protein homeostasis may be a key variable in explaining organismal robustness. Finally, our work provides an elegant example of harnessing the power of evolution and comparative genomics to address fundamental open questions in biology with direct relevance to human diseases.

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Thermal stress induces a distinct transcriptome profile in the Pacific oyster Crassostrea gigas

Cited by 34 publications

References 49 publications

Heat-resistant cytosolic malate dehydrogenases (cMDHs) of thermophilic intertidal snails (genus Echinolittorina): protein underpinnings of tolerance to body temperatures reaching 55°C

Heat-resistant cytosolic malate dehydrogenases (cMDHs) of thermophilic intertidal snails (genus Echinolittorina): protein underpinnings of tolerance to body temperatures reaching 55°C

Metabolic response of Scapharca subcrenata to heat stress using GC/MS-based metabolomics

Pervasive convergent evolution and extreme phenotypes define chaperone requirements of protein homeostasis

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