Vargula tsujii
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA552147 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR9308458_1.fastq.gz | Fastqsanger.gz | |||
| SRR9308458_2.fastq.gz | Fastqsanger.gz |
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Project description:Transcriptome analysis of sea firefly Vargula hilgendorfii
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Project description:The sea-firefly, Vargula hilgendorfii, is a bioluminescent crustacean
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Project description:Marine luciferases are regularly employed as useful reporter molecules across a range of various applications. However, attempts to transition expression from their native eukaryotic environment into a more economical prokaryotic, i.e. bacterial, expression system often presents several challenges. Specifically, bacterial protein expression inherently lacks chaperone proteins to aid in the folding process, while Escherichia coli presents a reducing cytoplasmic environment in. These conditions contribute to the inhibition of proper folding of cysteine-rich proteins, leading to incorrect tertiary structure and ultimately inactive and potentially insoluble protein. Vargula luciferase (Vluc) is a cysteine-rich marine luciferase that exhibits glow-type bioluminescence through a reaction between its unique native substrate and molecular oxygen. Because most other commonly used bioluminescent proteins exhibit flash-type emission kinetics, this emission characteristic of Vluc is desirable for high-throughput applications where stability of emission is required for the duration of data collection. A truncated form of Vluc that retains considerable bioluminescence activity (55%) compared to the native full-length protein has been reported in the literature. However, expression and purification of this luciferase from bacterial systems has proven difficult. Herein, we demonstrate the expression and purification of a truncated form of Vluc from E. coli. This truncated Vluc (tVluc) was subsequently characterized in terms of both its biophysical and bioluminescence properties.
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Project description:Bioluminescence, or the production of light by living organisms via chemical reaction, is widespread across Metazoa. Laboratory culture of bioluminescent organisms from diverse taxonomic groups is important for determining the biosynthetic pathways of bioluminescent substrates, which may lead to new tools for biotechnology and biomedicine. Some bioluminescent groups may be cultured, including some cnidarians, ctenophores, and brittle stars, but those use luminescent substrates (luciferins) obtained from their diets, and therefore are not informative for determination of the biosynthetic pathways of the luciferins. Other groups, including terrestrial fireflies, do synthesize their own luciferin, but culturing them is difficult and the biosynthetic pathway for firefly luciferin remains unclear. An additional independent origin of endogenous bioluminescence is found within ostracods from the family Cypridinidae, which use their luminescence for defense and, in Caribbean species, for courtship displays. Here, we report the first complete life cycle of a luminous ostracod (Vargula tsujii Kornicker & Baker, 1977, the California Sea Firefly) in the laboratory. We also describe the late-stage embryogenesis of Vargula tsujii and discuss the size classes of instar development. We find embryogenesis in V. tsujii ranges from 25-38 days, and this species appears to have five instar stages, consistent with ontogeny in other cypridinid lineages. We estimate a complete life cycle at 3-4 months. We also present the first complete mitochondrial genome for Vargula tsujii. Bringing a luminous ostracod into laboratory culture sets the stage for many potential avenues of study, including learning the biosynthetic pathway of cypridinid luciferin and genomic manipulation of an autogenic bioluminescent system.
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Project description:The marine ostracod Vargula hilgendorfii ejects luciferin and luciferase into seawater to produce a bright luminous cloud. The light is due to the oxidation of luciferin, an imidazopyrazine compound, by molecular oxygen, catalyzed by luciferase. The mechanism of the reaction has been studied extensively and the 60 kcal/mol required for the blue emission have been shown to be derived from the oxidation of luciferin via a dioxetanone intermediate, in which the excited state oxyluciferin bound to luciferase is the emitter. However, only limited information is available regarding the properties of the enzyme. This paper reports the cloning and sequence analysis of the cDNA for Vargula luciferase and the expression of the cDNA in a mammalian cell system. The primary structure, deduced from the nucleotide sequence, consists of 555 amino acid residues in a single polypeptide chain with a molecular weight of 62,171. Two regions of the enzyme show significant amino acid sequence homology with an N-terminal segment of the photoprotein aequorin. The Vargula luciferase gene, which contains a signal sequence for secretion, should be well suited as a reporter in studies of gene expression.
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Project description:An overview of small RNAs sequences existing in seed development and contrasted with vegetative tissues of the soybean
2012-10-09 | GSE36728 | GEO