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| Dataset | Description | Keywords | Number of Conditions | Reference |
|---|---|---|---|---|
| cAMP/PKA signaling balances respiratory activity with mitochondria dependent apoptosis via transcriptional regulation | This data provides evidence that elevation of cAMP levels has a dramatic effect on the transcriptome of yeast cells, with particular emphasis on mitochondrial function and the promotion of ROS production | organelles, biogenesis, structure, and function, oxidative stress | 8 | Leadsham JE and Gourlay CW (2010) PMID:21108829 |
| Cells following mtDNA loss, or NAR1 repression | Expression analysis of cells the given amount of time after mtDNA was lost (or Nar1 expression was repressed) compared to pretreatment (or NAR1 being fully expressed). | organelles, biogenesis, structure, and function, DNA replication, recombination and repair | 6 | Veatch JR, et al. (2009) PMID:19563757 |
| Endoplasmic reticulum–mitochondria junction is required for iron homeostasis | The Endoplasmic Reticulum–Mitochondria Encounter Structure (ERMES) is a protein complex that tethers the two organelles and creates the physical basis for communication between them. ERMES functions in lipid and calcium exchange between the ER and mitochondria, mitochondrial protein import and maintenance of mitochondrial morphology and genome. Here we report that ERMES is also required for iron homeostasis. Loss of ERMES components activates an Aft1-dependent iron deficiency response even in iron-replete conditions, leading to accumulation of excess iron inside the cell. This function is independent of ERMES known roles in calcium regulation, phospholipid biosynthesis or mitochondrial biology. A mutation in the vacuolar protein sorting 13 (VPS13) gene that rescues the glycolytic phenotype of ERMES mutants suppresses the iron deficiency response and iron accumulation. Our study reveals that proper communication between the ER and mitochondria is required for appropriate maintenance of cellular iron levels. | metal or metalloid ion utilization, organelles, biogenesis, structure, and function | 12 | Xue Y, et al. (2017) PMID:28637866 |
| Expression data from rho+ and rho0 budding yeast celles harvetsed from complete medium with 2% glucose before or after shifting to complete medium without glucose | This experiment compares mRNA expression in cells with and without mitochondrial DNA (_+ and _0 cells respectively) | fermentation, organelles, biogenesis, structure, and function | 12 | |
| Gene Expression Profile of app1Δpah1Δdpp1Δlpp1Δ | Deletion mutant of the yeast app1Δpah1Δdpp1Δlpp1Δ were studied for gene expression levels | organelles, biogenesis, structure, and function, lipid metabolism | 2 | |
| Integrative Omics reveals changes in the cellular landscape of yeast without peroxisomes | Peroxisomes are organelles that are crucial for cellular metabolism. However, these organelles play also important roles in non-metabolic processes, such as signalling. To uncover the consequences of peroxisome deficiency, we compared two extremes, namely Saccharomyces cerevisiae wild-type and pex3 cells, which lack functional peroxisomes, employing transcriptomics and quantitative proteomics technology. Cells were grown on acetate, a carbon source that involves peroxisomal enzymes of the glyoxylate cycle and does not repress peroxisomal proteins. Transcripts of peroxisomal β-oxidation genes and the corresponding proteins were enhanced in pex3 cells. Peroxisome-deficiency also caused reduced levels of membrane bound peroxins, while the soluble receptors Pex5 and Pex7 were enhanced at the protein level. In addition, we observed alterations in non-peroxisomal transcripts and proteins, especially mitochondrial proteins involved in respiration or import processes. Our results not only reveal the impact of the absence of peroxisomes in yeast, but also represent a rich resource of candidate genes/proteins that are relevant in peroxisome biology. | organelles, biogenesis, structure, and function | 6 | |
| Inter- and intra- chromosomal interactions change on a global scale according to the metabolic regime employed by Saccharomyces cerevisiae | Nuclear and mitochondrial organelles must maintain a communication system | organelles, biogenesis, structure, and function, transcription | 2 | Rodley CD, et al. (2012) PMID:22292080 |
| Long-read direct RNA sequencing of the mitochondrial transcriptome of Saccharomyces cerevisiae | Mitochondria fulfil many essential roles in eukaryotic cells, yet some of their molecular mechanisms are still unexplored. Although 99% of the mitochondrial proteins are imported from the cytosol, mitochondria have their own DNA, transcription and translation machinery. The Saccharomyces cerevisiae mitochondrial DNA contains 11 polycistronic transcripts that encode 2 ribosomal subunits, 24 tRNAs and 9 genes, which can be spliced in alternative ways to yield different proteins. There are still many unresolved questions about mitochondrial genes and their splicing, including how gene expression and splicing is affected by different growth conditions and what role introns play in mitochondrial physiology. In the present study, we aimed to elucidate this by developing an RNA-sequencing method for mitochondrial RNA using Nanopore technology. | transcriptome, organelles, biogenesis, structure, and function | 6 | Koster CC, et al. (2024) PMID:37642136 |
| Looking for mitochondrial associated RNA | We investigated the peripheral mitochondrial localization of nuclear-encoded mRNAs (MLR) in various conditions in which translation was inhibited or the mRNA binding protein context altered (Delta puf3) | organelles, biogenesis, structure, and function | 18 | Saint-Georges Y, et al. (2008) PMID:18523582 |
| Loss of subcellular lipid transport due to ARV1 deficiency disrupts organelle homeostasis and activates the unfolded protein response | The ARV1-encoded protein mediates sterol transport from the endoplasmic reticulum (ER) to the plasma membrane | response to unfolded protein, lipid metabolism, organelles, biogenesis, structure, and function | 14 | Shechtman CF, et al. (2011) PMID:21266578 |