Saccharomyces cerevisiae
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA302167 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR2921830.fastq.gz | Fastqsanger.gz | |||
| SRR2921831.fastq.gz | Fastqsanger.gz | |||
| SRR2921832.fastq.gz | Fastqsanger.gz | |||
| SRR2921833.fastq.gz | Fastqsanger.gz | |||
| SRR2921834.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 12 |
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Project description:Aneuploidy and aging are correlated; however, a causal link between these two phenomena has remained elusive. Here we show that yeast disomic for a single native yeast chromosome generally have a decreased replicative lifespan. In addition, the extent of this lifespan deficit correlates with the size of the extra chromosome. We identified a mutation in BUL1 that rescues both the lifespan deficit and a protein trafficking defect in yeast disomic for chromosome 5. Bul1 is an E4 ubiquitin ligase adaptor involved in a protein quality-control pathway that targets membrane proteins for endocytosis and destruction in the lysosomal vacuole thereby maintaining protein homeostasis. Concurrent suppression of the aging and trafficking phenotypes suggests that disrupted membrane protein homeostasis in aneuploid yeast may contribute to their accelerated aging. The data reported here demonstrate that aneuploidy can impair protein homeostasis, shorten lifespan, and may contribute to age-associated phenotypes.
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Project description:Aneuploidy and aging are correlated; however, a causal link between these two phenomena has remained elusive. Here we show that yeast disomic for a single native yeast chromosome generally have a decreased replicative lifespan. In addition, the extent of this lifespan deficit correlates with the size of the extra chromosome. We identified a mutation in BUL1 that rescues both the lifespan deficit and a protein trafficking defect in yeast disomic for chromosome 5. Bul1 is an E4 ubiquitin ligase adaptor involved in a protein quality-control pathway that targets membrane proteins for endocytosis and destruction in the lysosomal vacuole thereby maintaining protein homeostasis. Concurrent suppression of the aging and trafficking phenotypes suggests that disrupted membrane protein homeostasis in aneuploid yeast may contribute to their accelerated aging. The data reported here demonstrate that aneuploidy can impair protein homeostasis, shorten lifespan, and may contribute to age-associated phenotypes. These are all CGH arrays comparing DNA content between the indicated strain of interest and a wt control.
2015-12-04 | E-GEOD-75623 | biostudies-arrayexpress
Project description:Distinct stages of the translation elongation cycle revealed by sequencing ribosome-protected mRNA fragments
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Project description:In Saccharomyces cerevisiae, Pah1 phosphatidate (PA) phosphatase, which catalyzes the Mg2+-dependent dephosphorylation of PA to produce diacylglycerol, plays a key role in utilizing PA for the synthesis of membrane phospholipids or the neutral lipid triacylglycerol. Low activity favors phospholipid synthesis, whereas high activity favors triacylglycerol synthesis. Pah1 function is controlled by its subcellular location as regulated by phosphorylation and dephosphorylation. Multiple protein kinases phosphorylate Pah1 for its inactivation in the cytosol; Pah1 is activated via recruitment and dephosphorylation by the protein phosphatase Nem1-Spo7 at the nuclear/endoplasmic reticulum membrane where the PA phosphatase reaction occurs. Additionally, phosphorylation inhibits PA phosphatase activity and stabilizes Pah1 abundance, while dephosphorylation stimulates activity and destabilizes the enzyme abundance. Many of the protein kinases that phosphorylate Pah1 have yet to be characterized and their sites of phosphorylation defined. Here, we established Pah1 as a bona fide substrate of septin-associated Hsl1, a protein kinase involved in mitotic morphogenesis checkpoint signaling. Using Pah1 as substrate, Hsl1 activity was dependent on reaction time and the amounts of protein kinase, Pah1, and ATP. The phosphorylation occurred on Ser-748 and Ser-773, which together caused a 5-fold reduction in PA phosphatase catalytic efficiency. Analysis of cells expressing phosphorylation-deficient S748A and S773A mutant forms of Pah1 indicated that the Hsl1-mediated phosphorylation of Pah1 promoted membrane phospholipid synthesis at the expense of triacylglycerol, and ensured the dependence of Pah1 function on the Nem1-Spo7 protein phosphatase. This work advances understanding of how Hsl1 facilitates membrane phospholipid synthesis through the phosphorylation-mediated regulation of Pah1.
2024-06-13 | MSV000095027 | MassIVE
Project description:Proteostasis is a fundamental network of cellular pathways that ensures the optimal concentration and composition of correctly folded proteins within cells in normal and stress conditions. Among key components of this network are the molecular chaperones, which mediate protein folding but also act as modulators of protein synthesis. We have reported on a functional link between translation and de novo folding of proteins in the yeast Saccharomyces cerevisiae by uncovering a specific synthetic-lethal interaction between apparent unrelated mutant variants, the uL3[W255C] variant of the ribosomal protein uL3 and the null mutants of Zuo1 and Ssz1. Zuo1 and Ssz1 are components of the chaperone system named as ribosome-associated complex. Here, we performed a genome-wide analysis of ribosome dynamics by 5PSeq (Pelechano et al. 2015 PMID 2604644) in strains harbouring either wild-type uL3 or mutant uL3[W255C] in the presence or absence of Zuo1 or Ssz1. This method allows the study of ribosome dynamics, by sequencing 5’ phosphorylated mRNA co-translational degradation intermediates. Our results indicate that the rpl3[W255C] mutant is slightly impaired in translation elongation, defect that is significantly enhanced when combined with the deprivation of either Zuo1 or Ssz1.
2020-11-25 | GSE151632 | GEO