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The Circadian Protein Nocturnin Regulates Metabolic Adaptation in Brown Adipose Tissue

ABSTRACT: Fine-tuning of transcriptional responses can be critical for long-term outcomes in response to an environmental challenge. The circadian protein Nocturnin belongs to a family of proteins that include exonucleases, endonucleases and phosphatases and is most closely related to the CCR4 family of deadenylases that regulate the cellular transcriptome via control of polyA tail length of RNA transcripts. In this study, we investigate the role of Nocturnin in regulating the transcriptional response and downstream metabolic adaptations during cold exposure in brown adipose tissue. We find that Nocturnin exhibits dual localization within the cytosol and mitochondria, and loss of Nocturnin causes changes in expression of networks of mRNAs involved in mitochondrial function. Furthermore, Nocturnin-/- animals display significantly elevated levels of TCA cycle intermediates indicating that they have distinct metabolic adaptations during a prolonged cold exposure. We conclude that cold-induced stimulation of Nocturnin levels can regulate long-term metabolic adaptations to environmental challenges.

ORGANISM(S): Mus musculus

PROVIDER: GSE133050 | GEO | 2019/06/21

REPOSITORIES: GEO

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Project description:Leuconostoc lactis is found in vegetables, fruits, and meat and is used by the food industry in the preparation of dairy products, wines and sugars. We have previously demonstrated, that the dextransucrase (DsrLL) of Lc. lactis AV1n produces a high molecular weight dextran from sucrose, indicating its potential use as a dextran forming starter culture. We have also shown that this bacterium was able to produce 10-fold higher levels of dextran at 20 °C than at 37 °C, at the former temperature accompanied by an increase of dsrLL gene expression. However, the general physiological response of Lc. lactis AV1n to cold temperature in the presence of sucrose, leading to an increased production of dextran has not been yet investigated. Therefore, we have here used a quantitative proteomics approach to investigate the cold temperature-induced changes in the proteomic profile of this strain in comparison to its proteomic response at 37 °C. In total, 337 proteins were found to be differentially expressed at the applied significance criteria (FDR-adjusted p-value ≤ 0.05 and with a fold change ≥ 1.5 or ≤ 0.67) with 204 proteins overexpressed, among which 13% were involved in protein as well as cell wall, and envelope component biosynthesis including DsrLL as RNA chaperones. Proteins implicated in cold stress were expressed at high level at 20 °C and possibly play a role in the upregulation of DsrLL allowing efficient synthesis of the protein essential for its adaptation to cold. Post-transcriptional regulation of DsrLL expression also seems to take place through the interplay of exonucleases and endonucleases overexpressed at 20 °C, that would influence the half-life of the dsrLL transcript. Furthermore, the mechanism of cold resistance of Lc. lactis AV1n seems to be also based on energy saving through a decrease in growth rate mediated by a decrease in carbohydrate metabolism and its orientation towards the production pathways for storage molecules. Thus, this better understanding of the responses to low temperature and mechanisms for environmental adaptation of Lc. lactis could be exploited for industrial use of strains belonging to this species.

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The Circadian Protein Nocturnin Regulates Metabolic Adaptation in Brown Adipose Tissue

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