Coenzyme Q10 (CoQ10) or Ubiquinone10 (UQ10), an isoprenylated benzoquinone, is well-known for its role as an electron carrier in aerobic respiration. It is a sole representative of lipid soluble antioxidant that is synthesized in our body. In recent years, it has been found to be associated with a range of patho-physiological conditions and its oral administration has also reported to be of therapeutic value in a wide spectrum of chronic diseases. Additionally, as an antioxidant, it has been widely used as an ingredient in dietary supplements, neutraceuticals, and functional foods as well as in anti-aging creams. Since its limited dietary uptake and decrease in its endogenous synthesis in the body with age and under various diseases states warrants its adequate supply from an external source. To meet its growing demand for pharmaceutical, cosmetic and food industries, there is a great interest in the commercial production of CoQ10. Various synthetic and fermentation of microbial natural producers and their mutated strains have been developed for its commercial production. Although, microbial production is the major industrial source of CoQ10 but due to low yield and high production cost, other cost-effective and alternative sources need to be explored. Plants, being photosynthetic, producing high biomass and the engineering of pathways for producing CoQ10 directly in food crops will eliminate the additional step for purification and thus could be used as an ideal and cost-effective alternative to chemical synthesis and microbial production of CoQ10. A better understanding of CoQ10 biosynthetic enzymes and their regulation in model systems like E. coli and yeast has led to the use of metabolic engineering to enhance CoQ10 production not only in microbes but also in plants. The plant-based CoQ10 production has emerged as a cost-effective and environment-friendly approach capable of supplying CoQ10 in ample amounts. The current strategies, progress and constraints of CoQ10 production in plants are discussed in this review.
Objectives Human phospholipid scramblase 1 (hPLSCR1) is a multifunctional protein so it is vital to understand the regulation of its expression and transcription factors play critical role in regulating any gene.Results The transcription factor (TF) prediction tool ConSite identified one S-SOX5 binding site on the promoter region of hPLSCR1. Luciferase assays determined the increase in hPLSCR1 promoter activity with the increase in S-SOX5 concentration in a dose dependent manner. The deletion and the site-directed mutagenesis constructs exhibited a decrease in the hPLSCR1 promoter activity as compared to control. Also, transcriptional regulation of hPLSCR1 by S-SOX5 was checked by western blotting using S-SOX5 and hPLSCR1 specific antibodies. Further, Chromatin Immunoprecipitation (ChIP) assay confirmed the in-vivo interaction of S-SOX5 with hPLSCR1 promoter. Conclusions The expression of hPLSCR1 in HEK293T cells was shown to be upregulated by one S-SOX5 binding site present on the hPLSCR1 promoter suggesting that S-SOX5 as the potent regulator of hPLSCR1 expression.
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