Clitoria ternatea isolate:LY-2023
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ABSTRACT:
PROVIDER: PRJNA1016062 | ENA |
REPOSITORIES: ENA
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Project description:Clitoria ternatea Transcriptome or Gene expression
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Project description:Clitoria ternatea Transcriptome or Gene expression
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Project description:Clitoria ternatea Transcriptome or Gene expression
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Project description:Clitoria ternatea Genome sequencing and chromosome level assembly
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Project description:Clitoria ternatea isolate:Multiple tissues Transcriptome or Gene expression
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Project description:Clitoria ternatea cultivar:Milgarra Transcriptome or Gene expression
| PRJNA286977 | ENA
Project description:Flowers of the butterfly pea (Clitoria ternatea) accumulate a group of polyacylated anthocyanins, named ternatins, in their petals. The first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin, a reaction catalyzed in C. ternatea by UDP-glucose:anthocyanidin 3-O-glucosyltransferase (Ct3GT-A; AB185904). To elucidate the structure-function relationship of Ct3GT-A, recombinant Ct3GT-A was expressed in Escherichia coli and its tertiary structure was determined to 1.85 Å resolution by using X-ray crystallography. The structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like ?/?/? domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates. By comparing the structure of Ct3GT-A with that of the flavonoid glycosyltransferase VvGT1 from red grape (Vitis vinifera) in complex with UDP-2-deoxy-2-fluoro glucose and kaempferol, locations of the catalytic His-Asp dyad and the residues involved in recognizing UDP-2-deoxy-2-fluoro glucose were essentially identical in Ct3GT-A, but certain residues of VvGT1 involved in binding kaempferol were found to be substituted in Ct3GT-A. These findings are important for understanding the differentiation of acceptor-substrate recognition in these two enzymes.
| S-EPMC3795551 | biostudies-literature
Project description:Rhizobia were isolated from the root nodules of Clitoria ternatea in Thailand. The phylogeny of the isolates was investigated using 16S rDNA and the internal transcribed spacer (ITS) region from 16S to 23S rDNA. The phylogenetic tree of the 16S rDNA showed that ten of the eleven isolates belonged to Bradyrhizobium elkanii, and one belonged to Bradyrhizobium japonicum. The topology of the ITS tree was similar to that of 16S rDNA. The acetylene reduction activity was higher for the nodules inoculated with the isolated B. elkanii strains than for those inoculated with B. japonicum strains. When C. ternatea plants were inoculated with various Bradyrhizobium USDA strains isolated from Glycine max, C. ternatea formed many effective nodules with B. elkanii, especially USDA61. However, acetylene reduction activity per plant and the growth were higher in C. ternatea inoculated with our isolates. From these data we propose that effective rhizobia inoculant were identified for C. ternatea cultivation.
| S-EPMC6879394 | biostudies-literature
Project description:The perennial leguminous herb Clitoria ternatea (butterfly pea) has attracted significant interest based on its agricultural and medical applications, which range from use as a fodder and nitrogen fixing crop, to applications in food coloring and cosmetics, traditional medicine and as a source of an eco-friendly insecticide. In this article we provide a broad multidisciplinary review that includes descriptions of the physical appearance, distribution, taxonomy, habitat, growth and propagation, phytochemical composition and applications of this plant. Notable amongst its repertoire of chemical components are anthocyanins which give C. ternatea flowers their characteristic blue color, and cyclotides, ultra-stable macrocyclic peptides that are present in all tissues of this plant. The latter are potent insecticidal molecules and are implicated as the bioactive agents in a plant extract used commercially as an insecticide. We include a description of the genetic origin of these peptides, which interestingly involve the co-option of an ancestral albumin gene to produce the cyclotide precursor protein. The biosynthesis step in which the cyclic peptide backbone is formed involves an asparaginyl endopeptidase, of which in C. ternatea is known as butelase-1. This enzyme is highly efficient in peptide ligation and has been the focus of many recent studies on peptide ligation and cyclization for biotechnological applications. The article concludes with some suggestions for future studies on this plant, including the need to explore possible synergies between the various peptidic and non-peptidic phytochemicals.
| S-EPMC6546959 | biostudies-literature