Isolation of a FAD‐GPDH gene encoding a mitochondrial FAD‐dependent glycerol‐3‐phosphate dehydrogenase from <i>Dunaliella salina</i>

Yang, Wanggui; Cao, Yi; Sun, Xiaofei; Huang, Fei; He, Qinghua; Qiao, Dan; Bai, Linhan

doi:10.1002/jobm.200610263

Cited by 15 publications

(12 citation statements)

References 29 publications

(31 reference statements)

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“…This indicates that the, up-regulation of DsPFK expression occurs in order to satisfy the requirement of the massive synthesis of glycerol under hyperosmotic stress. The response of DsPFK to hyperosmotic stress is similar to that of DsFAD-GPDH and DsGPI [9,25]. Transcription levels first increased significantly and then decreased significantly, suggesting that the functions of DsPFK, DsFAD-GPDH and DsGPI are coordinated.…”

Section: Discussionmentioning

confidence: 72%

“…The content of intracellular dihydroxyacetone phosphate determines the rate and amount of the production of glycerol. Phosphofructokinase (PFK) [8] and glycerol-3-phosphate dehydrogenase (GPD) [9][10][11] are two key enzymes of this process. PFK catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate [12,13], and has the characteristics of allosteric modulation in bacteria, plants, and animals, keeping consistent with the activity of glycolysis [14].…”

Section: Introductionmentioning

confidence: 99%

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The relationship of glycerol and glycolysis metabolism patway under hyperosmotic stress in Dunaliella salina

et al. 2014

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This study detected the upstream and downstream key genes of glycolysis in Dunaliella Salina by using Real-time FluorescenceQuantitative PCR assays and measurement of enzyme activity. The results were as follows: the levels of transcription, enzyme activity, and protein of D. salina PFK were up-regulated under hyperosmotic stress while D. salina ENO were down-regulated. At the same time we monitored the change of intracellular degradation of starch, the synthesis of glycerol and PEP concentration in Dunaliella Salina under hyperosmotic stress. We found that lower expression of DsENO reduced the concentration of intracellular PEP which promoted the degradation of starch, and decreased the flow of carbon into the tricarboxylic acid cycle which would favor the synthesis of glycerol.

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Section: Discussionmentioning

confidence: 72%

Section: Introductionmentioning

confidence: 99%

The relationship of glycerol and glycolysis metabolism patway under hyperosmotic stress in Dunaliella salina

et al. 2014

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“…-GPDHs in Saccharomyces cerevisiae and Arabidopsis combine their activity with a mitochondrial FAD-dependent GPDH to form the G3P shuttle, which function seems to be transferring reducing equivalents from cytosol into the mitochondrial respiratory chain [19,29,31]. In microalgae, a mitochondrial FAD-GPDH has recently been identified for D. salina [41]. It will be interesting to investigate whether CrGPDH1 could be involved in a similar G3P shuttle in C. reinhardtii.…”

Section: Discussionmentioning

confidence: 97%

In Silico Cloning and Characterization of the Glycerol-3-Phosphate Dehydrogenase (GPDH) Gene Family in the Green Microalga Chlamydomonas reinhardtii

et al. 2012

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Glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the conversion of dihydroxyacetone phosphate (DHAP) and NADH to glycerol-3-phosphate (G3P) and NAD(+). G3P is important as a precursor for glycerol and glycerolipid synthesis in microalgae. A GPDH enzyme has been previously purified from the green microalga Chlamydomonas reinhardtii, however, no genes coding for GPDH have been characterized before. In this study, we report the in silico characterization of three putative GPDH genes from C. reinhardtii: CrGPDH1, CrGPDH2, and CrGPDH3. These sequences showed a significant similarity to characterized GPDH genes from the microalgae Dunaliella salina and Dunaliella viridis. The prediction of the three-dimensional structure of the proteins showed the characteristic fold topology of GPDH enzymes. Furthermore, the phylogenetic analysis showed that the three CrGPDHs share the same clade with characterized GPDHs from Dunaliella suggesting a common evolutionary origin and a similar catalytic function. In addition, the K(a)/K(s) ratios of these sequences suggested that they are under purifying selection. Moreover, the expression analysis showed a constitutive expression of CrGPDH1, while CrGPDH2 and CrGPDH3 were induced in response to osmotic stress, suggesting a possible role for these two sequences in the synthesis of glycerol as a compatible solute in osmoregulation, and perhaps also in lipid synthesis in C. reinhardtii. This study has provided a foundation for further biochemical and genetic studies of the GPDH family in this model microalga, and also opportunities to assess the potential of these genes to enhance the synthesis of TAGs for biodiesel production.

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“…; Yang et al . ). Both the transcription and enzyme activities of FAD‐dependent GPDH were shown to increase after 1–3 h but declined after 3–6 h of salt stress (Yang et al .…”

Section: Introductionmentioning

confidence: 97%

Characterization of genes and enzymes in Dunaliella salina involved in glycerol metabolism in response to salt changes

Zhao

Gong

Chen

et al. 2013

Phycological Research

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Summary Dunaliella salina (Dunal) Teod is an extremely halotolerant unicellular eukaryotic alga whose salt tolerance is thought to be related to glycerol metabolism. However, the regulation of different genes and enzymes under high salt stress conditions has not yet been investigated. In this study, glycerol metabolism was characterized after establishing the optimum salt stress conditions for D. salina Y6. As the salinity in the medium changed from 1 M to 3 M, the glycerol content increased sharply for 1–3 h and then gradually reached its maximum level after 24 h of salt stress (a 2.3‐fold increase). Semi‐quantitative reverse transcription‐polymerase chain reaction analysis showed that the transcription of the glucose‐6‐phosphate isomerase gene was not affected by salt stress, whereas the transcriptions of the fructose‐1, 6‐diphosphate aldolase gene, glycerol‐3‐phosphate dehydrogenase genes‐2 and ‐3, and the dihydroxyacetone reductase gene initially increased and then declined. Furthermore, the magnitude of the decline was greater than that of the increase, particularly for the dihydroxyacetone reductase gene. Enzyme activity analysis showed that the activity of the glucose‐6‐phosphate isomerase did not change significantly, whereas fructose‐1, 6‐diphosphate aldolase activity decreased to 63% and dihydroxyacetone reductase activity decreased to 31% after 24 h of salt stress. Therefore, we propose that while the regulation of salt for glycerol metabolism in D. salina is very complex, the reduced decomposition of glycerol helps its accumulation. Finally, we also propose that dihydroxyacetone reductase may be the key enzyme involved in the regulation of the glycerol metabolic pathway under salt stress conditions.

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Isolation of a FAD‐GPDH gene encoding a mitochondrial FAD‐dependent glycerol‐3‐phosphate dehydrogenase from Dunaliella salina

Cited by 15 publications

References 29 publications

The relationship of glycerol and glycolysis metabolism patway under hyperosmotic stress in Dunaliella salina

The relationship of glycerol and glycolysis metabolism patway under hyperosmotic stress in Dunaliella salina

In Silico Cloning and Characterization of the Glycerol-3-Phosphate Dehydrogenase (GPDH) Gene Family in the Green Microalga Chlamydomonas reinhardtii

Characterization of genes and enzymes in Dunaliella salina involved in glycerol metabolism in response to salt changes

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