| Literature DB >> 33247451 |
Li-Ping Peng1, Qing Hao2, Si-Qi Men1,3, Xi-Ruo Wang1,3, Wen-Yuan Huang3, Ning-Ning Tong1,3, Mo Chen3, Zheng-An Liu1, Xiao-Feng Ma3, Qing-Yan Shu1,3.
Abstract
Chalcone synthase (CHS) is the key enzyme in the flavonoid biosynthetic pathway and has been studied in many plants, but the function of the CHS gene has not been well characterized in Paeonia ostii. In this study, we obtained a CHS homolog gene from P. ostii, which possessed the putative conserved amino acids of chalcone synthase by multiple alignment analysis and demonstrated the highest expression in developing seeds. In vitro assays of the recombinant PoCHS protein confirmed enzymatic activity using malonyl-CoA and 4-coumaroyl-CoA as substrates, and the optimal pH and reaction temperature were 7.5 and 40 °C, respectively. Furthermore, ectopic over-expression of PoCHS in Arabidopsis up-regulated the expression levels of genes involved in seed development (ABI), glycolysis (PKp2, PDH-E1a, and SUS2/3), and especially fatty acid biosynthesis (BCCP2, CAC2, CDS2, FatA, and FAD3). This resulted in an increased unsaturated fatty acid content, especially α-linolenic acid, in transgenic Arabidopsis seeds. In this study, we examined the functions of CHS homolog of P. ostii and demonstrated its new function in seed fatty acid biosynthesis.Entities:
Keywords: Paeonia ostii; chalcone synthase (CHS); fatty acids; flavonoids; α-Linolenic acid
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Year: 2020 PMID: 33247451 DOI: 10.1111/ppl.13293
Source DB: PubMed Journal: Physiol Plant ISSN: 0031-9317 Impact factor: 4.500