Measuring the dependence of the yeast heat shock response on intracellular pH during stress
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ABSTRACT:
PROVIDER: PRJNA599929 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR10850801.fastq.gz | Fastqsanger.gz | |||
| SRR10850802.fastq.gz | Fastqsanger.gz | |||
| SRR10850803.fastq.gz | Fastqsanger.gz | |||
| SRR10850804.fastq.gz | Fastqsanger.gz | |||
| SRR10850805.fastq.gz | Fastqsanger.gz |
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Project description:Measuring the dependence of the yeast heat shock response on intracellular pH and translation during stress
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Project description:S. cerevisiae cells acidify when they experience stressful temperatures. To determine whether this heat-shock associated acidification is important for the cellular response, we manipulated intracellular pH, heat shocked cells, and sequenced the transcriptome.
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Project description:Amongst several amoebic species that colonize the human gut only Entamoeba histolytica is able to cause tissue damage in the intestine and other organs. Amoebic pathogenicity and virulence are commonly evaluated as the parasiteM-+s ability to produce liver abscesses in hamsters (ALAH). Some molecules involved in several functions that enable E. histolytica to invade and survive in the tissues have been identified and proposed as virulence factors. However, despite the fact that during early tissue invasion E. histolytica has to cope with toxic oxygen concentrations, little attention have received the mechanisms of oxygen resistance and its relationship with pathogenicity and virulence. In this work we compared the ability of virulent E. histolytica, non virulent E. histolytica and non pathogenic E. dispar to survive under physiological oxygen concentrations. Also, the effect of hyperoxia on the transcriptome, the oxygen reduction pathway, iron-sulfur protein oxidation, protein carbonylation and complement resistance was analyzed. Our results showed that a low oxygen reduction capacity plus high complement susceptibility contribute to the inability of E. dispar to survive during the early tissue invasion. On the other hand, under hyperoxia, the non virulent E. histolytica phenotype was associated with a defect in the up-regulation of genes of the heat-shock response which correlated with accumulation of oxidized proteins and irreversible PFOR inactivation. We conclude that maintenance of an intracellular hypoxic environment and up regulation of the heat-shock protein response for proper metabolic functioning are primary requirements for amoebic pathogenicity and virulence.
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Project description:Recombinant Escherichia coli cultures are used to manufacture numerous therapeutic proteins and industrial enzymes, where many of these processes use elevated temperatures to induce recombinant protein production. The heat-shock response in wild-type E. coli has been well studied. In this study, the transcriptome profiles of recombinant E. coli subjected to a heat-shock and to a dual heat-shock recombinant protein induction were examined. Most classical heat-shock protein genes were identified as regulated in both conditions. The major transcriptome differences between the recombinant and reported wild-type cultures were heavily populated by hypothetical and putative genes, which indicates recombinant cultures utilize many unique genes to respond to a heat-shock. Comparison of the dual stressed culture data with literature recombinant protein induced culture data revealed numerous differences. The dual stressed response encompassed three major response patterns: induced-like, in-between, and greater than either individual stress response. Also, there were no genes that only responded to the dual stress. The most interesting difference between the dual stressed and induced cultures was the amino acid-tRNA gene levels. The amino acid-tRNA genes were elevated for the dual cultures compared to the induced cultures. Since tRNAs facilitate protein synthesis via translation, this observed increase in amino acid-tRNA transcriptome levels, in concert with elevated heat-shock chaperones, might account for improved productivities often observed for thermo-inducible systems. Most importantly, the response of the recombinant cultures to a heat-shock was more profound than wild-type cultures, and further, the response to recombinant protein induction was not a simple additive response of the individual stresses. The objective of the present work is to gain a better understanding of the heat-shock response in recombinant cultures and how this response might impact recombinant protein production. To accomplish this objective, the transcriptome response of recombinant cultures subjected to a heat-shock and a dual heat-shock recombinant protein induction were analyzed. The transcriptome levels were determined using Affymetrix E. coli Antisense DNA microarrays, such that the entire genome was evaluated. These two transcriptome responses were also compared to recombinant cultures at normal growth temperature that were not over-expressing the recombinant protein and a set of literature recombinant culture data that were chemically induced to over-express the recombinant protein. Additionally, the heat-shock response of the recombinant cultures was compared to the literature report of the heat-shock response in wild-type cultures. The results of the global transcriptome analysis demonstrated that recombinant cultures respond differently to a heat-shock stress than wild-type cultures, where the transcriptome response of the recombinant cultures is further modified by production of a recombinant protein.
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