Two potential fish glycerol-3-phosphate phosphatases

Raymond, James A.

doi:10.1007/s10695-015-0048-7

Cited by 6 publications

(3 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S16B). Moreover, glycerol-3-phosphate phosphatase ( g3pp ), a crucial enzyme for glycerol biosynthesis (Raymond 2015) experienced an elevated rate of evolution (fig. 4B).…”

Section: Resultsmentioning

confidence: 99%

Multiple omic investigations of freeze tolerance adaptation in the aquatic ectothermic vertebrate, the Amur sleeper

Jiang

Qian

et al. 2022

Preprint

View full text Add to dashboard Cite

Freeze tolerance is an amazing overwintering strategy that enables ectotherms to occupy new niches and survive in cold climates. However, the genetic basis underpinning this ecologically relevant adaptation is largely unknown. Amur sleeper is the only known freeze-tolerant fish species that can overwinter with its entire body frozen in ice. Here, we sequenced the chromosome-level genome of the Amur sleeper and performed comparative genomic, transcriptomic, and metabolomic analyses to investigate this remarkable adaptation. Phylogenetic analyses showed that the Amur sleeper diverged from its close relative with no cold hardiness about 15.07 million years ago and revealed two unusual population expansions during the glacial epochs. Integrative omics data identified a synchronous regulation of genes and metabolites involved in hypometabolism and cellular stress response, and several related genes showed strong evidence of accelerated evolution and positive selection. Potential evolutionary innovations that might aid in freezing survival were found to be associated with the dynamic rearrangement of the cytoskeleton to maintain cell viability, redistribution of water and cryoprotectants to limit cell volume reduction, and inhibition in nerve activity to facilitate dormancy, demonstrating a coordinated evolution for this complex adaptation. Overall, our work provides valuable resources and opportunities to unveil the genetic basis of freeze tolerance adaptation in ectothermic vertebrates.

show abstract

“…S16B). Moreover, glycerol-3-phosphate phosphatase ( g3pp ), a crucial enzyme for glycerol biosynthesis (Raymond 2015) experienced an elevated rate of evolution (fig. 4B).…”

Section: Resultsmentioning

confidence: 99%

Multiple omic investigations of freeze tolerance adaptation in the aquatic ectothermic vertebrate, the Amur sleeper

Jiang

Qian

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

“…The transcript level of an uncharacterized phosphatase was elevated in isolated liver cells following 24 h after a transition from warm to cold temperature inducing glycerol synthesis and after 72 h expression level was 20-fold higher under cold than warm incubation ). More recently, Raymond (2015) has assembled two phosphatases from existing EST libraries. One of these transcripts matches the primers utilized by Hall et al 2011 in the study described above.…”

Section: Metabolic Control Of Glycerol Synthesis In Liver Final Stepsmentioning

confidence: 99%

Rainbow smelt: the unusual case of cryoprotection by sustained glycerol production in an aquatic animal

Driedzic

2015

J Comp Physiol B

View full text Add to dashboard Cite

Rainbow smelt flourish at -1.8 °C, the freezing point of sea water. An antifreeze protein contributes to freeze point depression but, more importantly, cryoprotection is due to an elevation in osmotic pressure, by the accumulation of glycerol. The lower the water temperature, the higher the plasma glycerol with levels recorded as high as 400 mmol l(-1). Glycerol freely diffuses out in direct relation to the glycerol concentration and fish may lose as much as 15% of their glycerol reserve per day. Glycerol levels decrease from a maximum in February/March while water temperature is still sub-zero. The decrease in glycerol may respond to a photoperiod signal as opposed to initiation which is triggered by low temperature. The initial increase in glycerol level is supported by liver glycogen but high sustained glycerol level is dependent upon dietary carbohydrate and protein. The metabolic pathways leading to glycerol involve flux from glycogen/glucose to the level of dihydroxyacetone phosphate (DHAP) via the initial part of glycolysis and from amino acids via a truncated gluconeogenesis again to the level of DHAP. DHAP in turn is converted to glycerol 3-phosphate (G3P) and then directly to glycerol. The key to directing DHAP to G3P is a highly active glycerol 3-P dehydrogenase. G3P is converted directly to glycerol via G3P phosphatase, the rate-limiting step in the process. The transition to glycerol production is associated with increased activities of enzymes at key loci in the top part of glycogenolysis/glycolysis. Curtailment of the final section of glycolysis may reside at the level of pyruvate oxidation with an inactivation of pyruvate dehydrogenase (PDH) driven by increased levels of PDH kinase. Enzymes associated with amino acid trafficking are elevated as is the pivotal enzyme phosphoenolpyruvate carboxykinase.

show abstract

“…Previous studies referred to the enzymes involved only generically without identifying specific genes, and thus not really "nailing down" the pathway. Recently, the specific enzymes involved in glycerol synthesis have been identified in a bacterium (Larrouy-Maumus et al, 2013), a fish (Raymond, 2015), and, as highlighted here, two species of algae (Morales-Sanchez et al, 2017;. The algal enzymes are especially interesting because of their novel form in which the two enzymes needed to convert DHAP into glycerol are fused into a single enzyme.…”

mentioning

confidence: 96%

Glycerol Is an Osmoprotectant in Two Antarctic Chlamydomonas Species From an Ice-Covered Saline Lake and Is Synthesized by an Unusual Bidomain Enzyme

2020

Self Cite

View full text Add to dashboard Cite

Glycerol, a compatible solute, has previously been found to act as an osmoprotectant in some marine Chlamydomonas species and several species of Dunaliella from hypersaline ponds. Recently, Chlamydomonas reinhardtii and Dunaliella salina were shown to make glycerol with an unusual bidomain enzyme, which appears to be unique to algae, that contains a phosphoserine phosphatase and glycerol-3-phosphate dehydrogenase. Here we report that two psychrophilic species of Chlamydomonas (C. spp. UWO241 and ICE-MDV) from Lake Bonney, Antarctica also produce high levels of glycerol to survive in the lake's saline waters. Glycerol concentration increased linearly with salinity and at 1.3 M NaCl, exceeded 400 mM in C. sp. UWO241, the more salt-tolerant strain. We also show that both species expressed several isoforms of the bidomain enzyme. An analysis of one of the isoforms of C. sp. UWO241 showed that it was strongly upregulated by NaCl and is thus the likely source of glycerol. These results reveal another adaptation of the Lake Bonney Chlamydomonas species that allow them to survive in an extreme polar environment.

show abstract

Two potential fish glycerol-3-phosphate phosphatases

Cited by 6 publications

References 27 publications

Multiple omic investigations of freeze tolerance adaptation in the aquatic ectothermic vertebrate, the Amur sleeper

Multiple omic investigations of freeze tolerance adaptation in the aquatic ectothermic vertebrate, the Amur sleeper

Rainbow smelt: the unusual case of cryoprotection by sustained glycerol production in an aquatic animal

Glycerol Is an Osmoprotectant in Two Antarctic Chlamydomonas Species From an Ice-Covered Saline Lake and Is Synthesized by an Unusual Bidomain Enzyme

Contact Info

Product

Resources

About