Saccharomyces cerevisiae
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA396952 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR5891410.fastq.gz | Fastqsanger.gz | |||
| SRR5891420.fastq.gz | Fastqsanger.gz | |||
| SRR5891411.fastq.gz | Fastqsanger.gz | |||
| SRR5891421.fastq.gz | Fastqsanger.gz | |||
| SRR5891412.fastq.gz | Fastqsanger.gz |
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Similar Datasets
Project description:Spontaneous mutations in CYC8 and MIG1 suppress the short chronological lifespan of budding yeast lacking SNF1/AMPK
| PRJNA433655 | ENA
Project description:Chronologically aging yeast cells are prone to adaptive regrowth, whereby mutants with a survival advantage spontaneously appear and re-enter the cell cycle in stationary phase cultures. Adaptive regrowth is especially noticeable with short-lived strains, including those defective for SNF1, the homolog of mammalian AMP-activated protein kinase (AMPK). SNF1 becomes active in response to multiple environmental stresses that occur in chronologically aging cells, including glucose depletion and oxidative stress. SNF1 is also required for the extension of chronological lifespan (CLS) by caloric restriction (CR) as defined as limiting glucose at the time of culture inoculation. To identify specific downstream SNF1 targets responsible for CLS extension during CR, we screened for adaptive regrowth mutants that restore chronological longevity to a short-lived snf1∆ parental strain. Whole genome sequencing of the adapted mutants revealed missense mutations in TPR motifs 9 and 10 of the transcriptional co-repressor Cyc8 that specifically mediate repression through the transcriptional repressor Mig1. Another mutation occurred in MIG1 itself, thus implicating the activation of Mig1-repressed genes as a key function of SNF1 in maintaining CLS. Consistent with this conclusion, the cyc8 TPR mutations partially restored growth on alternative carbon sources and significantly extended CLS compared to the snf1∆ parent. Furthermore, cyc8 TPR mutations reactivated multiple Mig1-repressed genes, including the transcription factor gene CAT8, which is responsible for activating genes of the glyoxylate and gluconeogenesis pathways. Deleting CAT8 completely blocked CLS extension by the cyc8 TPR mutations on CLS, identifying these pathways as key Snf1-regulated CLS determinants.
2018-03-28 | GSE110409 | GEO
Project description:The highly conserved heterotrimeric protein kinase SNF1 is important for metabolic adaptations in the pathogenic yeast Candida albicans. A key function of SNF1 is to inactivate the repressor protein Mig1 and thereby allow the expression of genes that are required for the the utilization of alternative carbon sources when the preferred carbon source glucose is absent or becomes limiting. However, how SNF1 controls Mig1 activity in C. albicans has remained elusive. Using a phosphoproteomic approach, we found that Mig1 is phosphorylated at multiple serine residues. Replacement of these serine residues by nonphosphorylatable alanine residues strongly increased the repressor activity of Mig1 in cells lacking a functional SNF1 complex, indicating that additional protein kinases are involved in the regulation of Mig1. Unlike wild-type Mig1, whose levels strongly decreased when the cells were grown on sucrose or glycerol instead of glucose, the levels of a mutant Mig1 protein lacking nine phosphorylation sites remained high under these conditions. Despite the increased protein levels and the absence of multiple phosphorylation sites, cells with a functional SNF1 complex could still sufficiently inhibit the hyperactive Mig1 to enable wild-type growth on alternative carbon sources. In line with this, phosphorylated forms of the mutant Mig1 were still detected in the presence and absence of a functional SNF1, demonstrating that Mig1 contains additional, unidentified phosphorylation sites and that downstream protein kinases are involved in the control of Mig1 activity by SNF1.
2023-10-27 | PXD045393 | Pride
Project description:Snf1/AMPK functions as a heterotrimeric complex, consisting of a regulatory subunit that is senses the energy status, a catalytic subunit with the canonical kinase domain and a scaffolding subunit to secure the complex together. The high degree of conservation in the sequence, structure and function of yeast Snf1 and mammalian AMPK, it is only logical to investigate the extent of conservation in the downstream effects that are controlled by these kinases.
2020-12-18 | GSE29358 | GEO
Project description:Studies of aging and longevity are revealing how diseases that shorten life can be controlled to improve the quality of life and lifespan itself. Two strategies under intense study to accomplish this goal are rapamycin treatment and calorie restriction. New strategies are being discovered including one that uses low-dose myriocin treatment. Myriocin inhibits the first enzyme in sphingolipid synthesis in all eukaryotes and we showed recently that low-dose myriocin treatment increases yeast lifespan at least in part by down-regulating the sphingolipid-controlled Pkh1/2-Sch9 (ortholog of mammalian S6 kinase) signaling pathway. Here we show that myriocin treatment has global influences and modulates the evolutionarily conserved Snf1/AMPK, PKA and TORC1 signaling pathways to enhance yeast lifespan. These extensive affects of myriocin rival those of rapamycin and calorie restriction. Our studies in yeast along with other studies in mammals reveal the potential of myriocin or related compounds to lower the incidence of age-related diseases in humans. No-myriocin-treated cells and myriocin-treated cells; three biological replicates in each treatment
2014-09-22 | E-GEOD-41362 | biostudies-arrayexpress
Project description:The conserved Snf1/AMPK (AMP-activated protein Kinase) family is one of the central components in nutrient sensing and regulation of carbon metabolism in eukaryotes. It is also involved in several other processes such as stress resistance, invasive growth and ageing. Snf1 kinase is composed of a catalytic alpha-subunit Snf1, a regulatory gamma-subunit Snf4 and one of three possible beta-subunits, Sip1, Sip2 or Gal83. We used a systematic approach to study the role of the three beta-subunits by analyzing all 7 possible combinations of beta-subunit deletions together with the reference strain.
2010-05-27 | E-GEOD-20591 | biostudies-arrayexpress
Project description:Studies of aging and longevity are revealing how diseases that shorten life can be controlled to improve the quality of life and lifespan itself. Two strategies under intense study to accomplish this goal are rapamycin treatment and calorie restriction. New strategies are being discovered including one that uses low-dose myriocin treatment. Myriocin inhibits the first enzyme in sphingolipid synthesis in all eukaryotes and we showed recently that low-dose myriocin treatment increases yeast lifespan at least in part by down-regulating the sphingolipid-controlled Pkh1/2-Sch9 (ortholog of mammalian S6 kinase) signaling pathway. Here we show that myriocin treatment has global influences and modulates the evolutionarily conserved Snf1/AMPK, PKA and TORC1 signaling pathways to enhance yeast lifespan. These extensive affects of myriocin rival those of rapamycin and calorie restriction. Our studies in yeast along with other studies in mammals reveal the potential of myriocin or related compounds to lower the incidence of age-related diseases in humans.
2014-09-22 | GSE41362 | GEO
Project description:The conserved Snf1/AMPK (AMP-activated protein Kinase) family is one of the central components in nutrient sensing and regulation of carbon metabolism in eukaryotes. It is also involved in several other processes such as stress resistance, invasive growth and ageing. Snf1 kinase is composed of a catalytic α-subunit Snf1, a regulatory γ-subunit Snf4 and one of three possible β-subunits, Sip1, Sip2 or Gal83. We used a systematic approach to study the role of the three β-subunits by analyzing all 7 possible combinations of β-subunit deletions together with the reference strain.
2010-05-10 | GSE20591 | GEO
Project description:Aging and age-related neurodegeneration are among the major challenges because of the progressive increase in the number of elder people in the wold population. Nutrition, which has important long-term consequences for health, is actually considered a means to prevent diseases and to reach a healthy aging. Here we investigate the role of Vigna unguiculata beans on senescence by using Saccharomyces cerevisiae and Drosophila melanogaster as model systems. Aqueous extract, mainly containing starch, proteins and amino acids, extends chronological lifespan in yeast cells, showing a remarkable synergistic effect in combination with caloric restriction. The extension of yeast longevity requires both the anti-aging Snf1/AMPK and the pro-aging Ras2/PKA pathways. A significant marked increase of lifespan was observed also in fruit flies supplemented with the V. unguiculata extract, which is accompanied by the increased expression of FOXO, NOTCH, SIRT1 and heme oxygenase (HO) genes, already known to be required for the extension of fruit fly longevity. α-synuclein forms toxic intracellular protein inclusions in Parkinson’s disease (PD) and actually preventing α-synuclein self-assembly has become one of the most promising approaches for the treatment of this neurodegenerative disorder. Here, we report that in vitro aggregation of -synuclein, as well as its toxicity in yeast and in neuroblastoma cells, are strongly decreased in the presence of bean extract. In addition, in a Caenorhabditis elegans model of PD that expresses α-synuclein, Vigna unguiculate extract substantially reduces the number of the age-dependent degeneration of the cephalic dopaminergic neurons. Overall, our data support the role of Vigna unguiculata beans as a functional food, worth to be further explored in order to develop lead molecules for therapeutic intervention in age-related disorders.
2021-09-08 | PXD017716 | Pride
Project description:Cells are often exposed to physical or chemical stresses that can damage the structures of essential biomolecules. Stress-induced cellular damage can become deleterious if not managed appropriately. Rapid and adaptive responses to stresses are therefore crucial for cell survival. In eukaryotic cells, different stresses trigger post-translational modification of proteins with the small ubiquitin-like modifier SUMO. However, the specific regulatory roles of sumoylation in each stress response are not well understood. Here, we examined the sumoylation events that occur in budding yeast after exposure to hyperosmotic stress. We discovered by proteomic and biochemical analyses that hyperosmotic stress incurs the rapid and transient sumoylation of Cyc8 and Tup1, which together form a conserved transcription corepressor complex that regulates hundreds of genes. Gene expression and cell biological analyses revealed that sumoylation of each protein directs distinct outcomes. In particular, we discovered that Cyc8 sumoylation prevents the persistence of hyperosmotic stress-induced Cyc8-Tup1 inclusions, which involves a glutamine-rich prion domain in Cyc8. We propose that sumoylation protects against persistent inclusion formation during hyperosmotic stress, allowing optimal transcriptional function of the Cyc8-Tup1 complex.
2016-09-27 | GSE57476 | GEO