Acorus calamus var. americanus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA255036 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR1509372_1.fastq.gz | Fastqsanger.gz | |||
| SRR1509372_2.fastq.gz | Fastqsanger.gz | |||
| SRR1509373_1.fastq.gz | Fastqsanger.gz | |||
| SRR1509373_2.fastq.gz | Fastqsanger.gz |
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Project description:Acorus calamus var. americanus Transcriptome or Gene expression
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Project description:A new sesquiterpene, named neo-acorane A (1), and two known ones, acoric acid (2) and calamusin D (3), were isolated from a 95% ethanol extract of the rhizome parts of Acorus calamus L. Their structures were elucidated by spectroscopic methods, and the absolute configurations were determined by single-crystal X-ray diffraction analysis. Compounds 1 and 2 are nonisoprenoid sesquiterpenoids, likely biosynthesized from an acorane-type sesquiterpene by oxidative fission of the six- or five-membered ring. Moreover, compounds 1 (10 μM), 2 (5 μM and 10 μM) and 3 (10 μM) showed cell proliferation activity on the SK-N-BE (2) cell line.
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Project description:Background and aimsPlants have evolved a number of inducible defence mechanisms against pathogen attack, including synthesis of pathogenesis-related proteins. The aim of the study was to purify and characterize antifungal protein from leaves of Acorus calamus.MethodsLeaf proteins from A. calamus were fractionated by cation exchange chromatography and gel filtration and the fraction inhibiting the hyphal extension of phytopathogens was characterized. The temperature stability and pH optima of the protein were determined and its presence was localized in the leaf tissues.Key resultsThe purified protein was identified as a class III haem peroxidase with a molecular weight of approx. 32 kDa and pI of 7.93. The temperature stability of the enzyme was observed from 5 degrees C to 60 degrees C with a temperature optimum of 36 degrees C. Maximum enzyme activity was registered at pH 5.5. The pH and temperature optima were corroborated with the antifungal activity of the enzyme. The enzyme was localized in the leaf epidermal cells and lumen tissues of xylem, characteristic of class III peroxidases. The toxic nature of the enzyme which inhibited hyphal growth was demonstrated against phytopathogens such as Macrophomina phaseolina, Fusarium moniliforme and Trichosporium vesiculosum. Microscopic observations revealed distortion in the hyphal structure with stunted growth, increased volume and extensive hyphal branching.ConclusionsThis study indicates that peroxidases may have a role to play in host defence by inhibiting the hyphal extension of invading pathogens.
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Project description:Transcriptional profiling of larval stage I - IV of Homarus americanus, for assessment of stage specific developmental gene expression. Individuals from each stage were gathered in July of 2009 and 2010. A reference design was used to permit comparison of all stages. Study aims included assessment of global gene expression of larval development of healthy larvae, and identifying novel molecular pathways involved in H. americanus development.
2013-12-31 | GSE45683 | GEO
Project description:The American lobster, Homarus americanus, is not only of considerable economic importance but has also emerged as a pivotal model in neuroscience research. Neuropeptides, an important class of cell-to-cell signaling molecules, play crucial roles in a wide array of physiological and psychological processes. In light of the recently sequenced high-quality draft genome of the American lobster, our study sought to profile the neuropeptidome in this model organism. Employing advanced mass spectrometry techniques alongside functional genomic analysis, we identified 24 neuropeptide precursors and 101 unique mature neuropeptides in Homarus americanus. Intriguingly, 67 of these neuropeptides were discovered for the first time. Our findings offer a comprehensive overview of the peptidomic attributes of the lobster's nervous system and highlight the tissue-specific distribution of these neuropeptides. Collectively, this research not only enriches our understanding of the neural complexities of the American lobster but also sets a foundational basis for future investigations into the functional roles that these peptides play in crustacean species.
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