Arabidopsis thaliana
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA174789 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR566601.fastq.gz | Fastqsanger.gz | |||
| SRR566602.fastq.gz | Fastqsanger.gz | |||
| SRR566603.fastq.gz | Fastqsanger.gz | |||
| SRR566604.fastq.gz | Fastqsanger.gz |
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Project description:HSC70 is the cytosolic isoform of plant HSP70. We have found that HSC70 family proteins bind to the heat shock transcription factor A1s (HsfA1s), which are the master regulators of the heat shock response in plants, and suppress their activity. We additionally found that the triple knock out of HSC70s alters responses of Arabidopsis plants to salt stress. To investigate the role of the HSC70s in salt stress responses, we evaluated the effects of the triple knock out on the transcriptome under salt stress.
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Project description:Environmental stress, such as oxidative or heat stress, induces the activation of the heat shock response
(HSR) and leads to an increase in the heat shock proteins (HSPs) level. These HSPs act as molecular
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regulatory network of the HSR that reproduces quantitatively different heat shock experiments both
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Sivéry, A., Courtade, E., Thommen, Q. (2016). A minimal titration model of the mammalian dynamical heat shock response. Physical biology, 13(6), 066008.
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Project description:Regulation of the Arabidopsis Transcriptome by Oxidative Stress
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Project description:Differential regulation of HSFA1s and HSFA2 after heat shock in Arabidopsis
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Project description:HSC70 is the cytosolic isoform of plant HSP70. We have found that HSC70 family proteins bind to the heat shock transcription factor A1s (HsfA1s), which are the master regulators of the heat shock response in plants, and supress their activity. To investigate the role of HSC70s in the regulation of HsfA1s and heat shock responses, we evaluated the effect of triple knock out of HSC70s on the transcriptome under the normal growth condition.
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Project description:Genome-wide mapping of the Arabidopsis thaliana heat shock transcription factor A1b binding sites under non-stress and heat stress conditions [ChIP-seq]
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Project description:Transcriptional profiling of arsenic-induced toxicity and tolerance in Arabidopsis plants of different ecotypes Arsenic (As) is a toxic metalloid found ubiquitously in the environment and has widely been known as an acute poison and carcinogen. As toxicity is a major factor leading to root growth inhibition in plants. However, the molecular mechanisms of plants in response to As has not been extensively characterized. In this study, Arabidopsis ecotypes that are As-tolerant (Col-0) and -sensitive (Ws-2) were used to conduct a transcriptome analysis of the response to As (V). To begin elucidating the molecular basis of As toxicity and tolerance in Arabidopsis, seedlings of Col-0 and Ws-2 were subjected to As treatment. The root elongation rate of Col-0 was significantly higher than that of Ws-2 when exposed to As. The tolerant ecotype (Col-0) demonstrated lower accumulation of As when compared to the responses observed in the sensitive Ws-2. Subsequently, the effect of As exposure on genome-wide gene expression was examined in the two ecotypes. Comparative analysis of microarray data identified groups of genes with common and specific responses to As between Col-0 and Ws-2. The genes related to heat responses and oxidative stresses belonged to common responses, indicating conserved stress-associated changes across two ecotypes. The majority of specific responsive genes were those encoding heat shock proteins, heat shock factors, ubiquitin and transporters. The data suggested that metal transport and maintenance of protein structure may be important mechanisms for toxicity and tolerance to As. This study presents comprehensive surveys of global transcriptional regulation and identifies stress- and tolerance-associated genes in response to As. Comparison of Arabidopsis ecotype Col-0 and Ws-2 in response to As with the Affymetrix GeneChip were performed by the Affymetrix Gene Expression Service Lab (http://ipmb.sinica.edu.tw/affy/), supported by Academia Sinica, Taiwan
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