Journal article
Transcriptome analysis of Haematococcus pluvialis of multiple defensive systems against nitrogen starvation
Enzyme and microbial technology, Vol.134, pp.109487-109487
03/2020
Handle:
https://hdl.handle.net/2376/117877
PMID: 32044034
Abstract
Haematococcus pluvialis could accumulate large amounts of triacylglycerol (TAG) and astaxanthin under various environmental stresses. To gain insights into the multiple defensive systems for carbon metabolism against nitrogen starvation, transcriptome analysis was performed. It was found that the genes related to carbon fixation, glycolysis, fatty acid and carotenoid biosynthesis pathways were up-regulated remarkably. Glyceraldehyde 3-phosphate (G3P) biosynthesis was accelerated with the enhanced C3 and C4 pathway. Meanwhile, the pyruvate kinase (PK) and pyruvate dehydrogenase E2 component (aceF) genes were significantly increased 12.9-fold and 13.9-fold, respectively, resulting more pyruvate and acetyl-CoA generation, which were beneficial to carotenoids and fatty acid biosynthesis. Methylerythritol 4-phosphate (MEP) pathway mediated carotenoid precursor isopentenyl diphosphate (IPP) synthesis, as the all eight related genes were up-regulated. The carbon flux toward astaxanthin biosynthesis with the increased astaxanthin pathway genes. The redistribution of carbon was also promoted for TAG accumulation. In addition, the up-regulation of diacylglycerol acyltransferase (DGAT) and phospholipid: diacylglycerol acyltransferase (PDAT) genes indicated that both acyl-CoA dependent and independent pathway regulated TAG accumulation. Therefore, this work reveals the multiple defensive mechanism for carbon metabolism in response to nitrogen starvation, which extended our understanding on the carotenoids, TAG and other important metabolites synthesis.
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Details
- Title
- Transcriptome analysis of Haematococcus pluvialis of multiple defensive systems against nitrogen starvation
- Creators
- Yue Zhao - College of Life Science, North China University of Science and Technology, Tangshan, China; Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaYuyong Hou - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaWenjing Chai - College of Life Science, North China University of Science and Technology, Tangshan, China; Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaZhiyong Liu - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaXuan Wang - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaChunQing He - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaZhipeng Hu - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaShulin Chen - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, ChinaWeijie Wang - College of Life Science, North China University of Science and Technology, Tangshan, China. Electronic address: weijiewang@ncst.edu.cnFangjian Chen - Tianjin Key Laboratory for Industrial Biological Systems and Bioprocessing Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China. Electronic address: chen_fj@tib.cas.cn
- Publication Details
- Enzyme and microbial technology, Vol.134, pp.109487-109487
- Academic Unit
- Biological Systems Engineering, Department of
- Identifiers
- 99900583054801842
- Language
- English
- Resource Type
- Journal article