Subjects: Agriculture, Forestry,Livestock & Aquatic Products Science >> Plant Protection submitted time 2018-07-18 Cooperative journals: 《广西植物》
Abstract： Dysphania schraderiana, in the Chenopodiaceae family, is widely distributed in Lhasa (Tibet, China) and used as a traditional medicine. The essential oil of Dysphania schraderiana, which contains abundant sesquiterpenes compounds, appeared to possess potential medicinal value. Farnesyl pyrophosphate synthase (FPPS) is a key branch-point enzyme in biosynthesis of terpene. In order to reveal D. schraderiana FPPS gene, the transcriptome database of D. schraderiana was mined and two gene sequences (DsFPPS1 and DsFPPS2) were obtained in this research. Subsequential protein physicochemical property, architectural feature, function and phylogeny relationship analysis of DsFPPSs were also predicted and analyzed. The results indicated that DsFPPS1 and DsFPPS2 sequences contained an ORF span of 1029 bp and 969 bp respectively, encoding 342 (DsFPPS1) and 322 (DsFPPS2) amino acids respectively.The analysis of amino acid composition indicated that the dominant components of DsFPPS1 and DsFPPS2 are both nonpolar amino acids. The molecular weight of DsFPPS1 and DsFPPS2 were 39.68 kD and 36.76 kD, respectively. Isoelectric point were 5.11 and 5.65 for DsFPPS1 and DsFPPS2, respectively. Besides, DsFPPS1 protein was predicted to be a stable protein, but DsFPPS2 protein was predicted to be an unstable protein. The amino acid sequence analysis showed that DsFPPS1 and DsFPPS2 had no signal peptide and transmembrane region. The possible localization of DsFPPS1 and DsFPPS2 was both in mitochondria. DsFPPS1 and DsFPPS2 protein exhibited 60.53% sequence identity, and possessed five conserved domain (Ⅰ~Ⅴ) and two characteristic Asp-rich motifs (DDXXD). The amino acid sequence of DsFPPS1 has higher homology with Chenopodium quinoa, Spinacia oleracea and Beta vulgaris than DsFPPS2. In addition, the secondary structure of DsFPPS proteins mainly consisted of α-helixes, which resulted in a bundle of 8 α-helices in tertiary structure. However, tertiary structure analysis showed that DsFPPS2 protein was missing an α-helix compared to DsFPPS1 protein. The result of phylogenetic analysis indicated that phylogenetic relationships of DsFPPS1 protein were closer to Chenopodiaceae plants consistent with sequence alignment results, while DsFPPS2 protein was clustered alone in phylogenetic tree. In general, these results could lay a foundation for an insight to molecular functionofDsFPPSandthesynthetic biologyofsesquiterpenesinD. schraderiana.
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