Nitzschia putrida strain:NIES-4239
Ontology highlight
ABSTRACT:
PROVIDER: PRJDB11016 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| DRR265429_1.fastq.gz | Fastqsanger.gz | |||
| DRR265429_2.fastq.gz | Fastqsanger.gz | |||
| DRR265430_1.fastq.gz | Fastqsanger.gz | |||
| DRR265430_2.fastq.gz | Fastqsanger.gz | |||
| DRR265431_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 28 |
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Project description:When grown under phosphate (Pi) deficiency, plants adjust their developmental program and metabolic activity to cope with this nutritional stress. For Arabidopsis, the developmental responses include inhibition of primary root growth and enhanced formation of lateral roots and root hairs. Pi deficiency also inhibits photosynthesis by suppressing the expression of photosynthetic genes. Interestingly, early studies showed that photosynthetic gene expression was also suppressed in roots, a non-photosynthetic tissue. The biological relevance of this phenomenon, however, is not known. In this work, we characterized an Arabidopsis mutant, hps7, which is hypersensitive to Pi deficiency; the hypersensitivity includes an increased inhibition of root growth. HPS7 encodes a tyrosylprotein sulfotransferase (TPST). Accumulation of TPST proteins, but not mRNA, is induced by Pi deficiency. Comparative RNA-Seq analyses indicated that expression of many photosynthetic genes was activated in the roots of hps7. Under Pi deficiency, the expression of the photosynthetic genes in hps7 is further increased, which leads to the enhanced accumulation of chlorophyll, starch, and reactive oxygen species. The increased inhibition of root growth in hps7 under Pi deficiency was completely reversed by growing plants in the dark. Based on these results, we propose that suppression of photosynthetic gene expression in roots is required for sustained root growth under Pi deficiency.
2014-07-28 | E-MTAB-4405 | biostudies-arrayexpress
Project description:The oceanic diatom Pseudo-nitzschia granii was cultured in the laboratory under steady-state iron-replete and iron-limited conditions. Transcriptomic and proteomic analyses were performed to determine how this organism reorganizes major metabolic processes as a function of iron supply.
2018-08-21 | PXD009698 | Pride
Project description:Biological relevance and intent of the experiment: Given their abundance in the oceans and the exceptional adaptive capacities that make them capable of colonizing the most disparate habitats, diatoms constitute a group of microalgae of considerable ecological importance. This experiment aims to provide a molecular characterization of sexual reproduction for the diatom Pseudo-nitzschia multistriata, in relation to the consumption of nutrients and the impact on the marine ecosystem, by exploring the gene expression changes occurring at different time points in the cells involved in the process. Experimental workflow: Cell cultures of P. multistriata belonging to opposite mating types (MT- and MT+) were grown in 12L/12D cycles at 18°C under normal light conditions (60 uE) and crossed at a final cell density of 20.000 cells/ml using half volume from each MT. Samples for transcriptomic analyses were collected at three time points for sexually reproducing cells (1 hour: T1, 24 hours: T2 and 120 hours: T3), and at one time point (24 hours: T2) for parental monocultures grown in parallel as control condition.
2021-11-24 | E-MTAB-8854 | biostudies-arrayexpress
Project description:BackgroundChitosanases (EC 3.2.1.132) hydrolyze the polysaccharide chitosan, which is composed of partially acetylated beta-(1,4)-linked glucosamine residues. In nature, chitosanases are produced by a number of Gram-positive and Gram-negative bacteria, as well as by fungi, probably with the primary role of degrading chitosan from fungal and yeast cell walls for carbon metabolism. Chitosanases may also be utilized in eukaryotic cell manipulation for intracellular delivery of molecules formulated with chitosan as well as for transformation of filamentous fungi by temporal modification of the cell wall structures.However, the chitosanases used so far in transformation and transfection experiments show optimal activity at high temperature, which is incompatible with most transfection and transformation protocols. Thus, there is a need for chitosanases, which display activity at lower temperatures.ResultsThis paper describes the isolation of a chitosanase-producing, cold-active bacterium affiliated to the genus Janthinobacterium. The 876 bp chitosanase gene from the Janthinobacterium strain was isolated and characterized. The chitosanase was related to the Glycosyl Hydrolase family 46 chitosanases with Streptomyces chitosanase as the closest related (64% amino acid sequence identity). The chitosanase was expressed recombinantly as a periplasmic enzyme in Escherichia coli in amounts about 500 fold greater than in the native Janthinobacterium strain. Determination of temperature and pH optimum showed that the native and the recombinant chitosanase have maximal activity at pH 5-7 and at 45 degrees C, but with 30-70% of the maximum activity at 10 degrees C and 30 degrees C, respectively.ConclusionsA novel chitosanase enzyme and its corresponding gene was isolated from Janthinobacterium and produced recombinantly in E. coli as a periplasmic enzyme. The Janthinobacterium chitosanase displayed reasonable activity at 10 degrees C to 30 degrees C, temperatures that are preferred in transfection and transformation experiments.
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Project description:Genotyping By Sequencing For Estimating Relative Abundances Of Diatom Taxa In Mock Communities
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