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Ola1p trafficking indicates an interaction network between mitochondria, Lipid droplets and stress granules in times of stress

ABSTRACT: Protein aggregates arise naturally under normal physiological conditions, but their formation is accelerated by age or stress-induced protein misfolding. One of the proteins that accumulate upon stress in yeast cells is Ola1p, know as the “super aggregator” Using a proximity labelling approach based upon the biotin ligase TurboID we were able to show that these Ola1p harbouring aggregates are, in fact, stress granules that interact with both mitochondria and LDs.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Peter Briza

LAB HEAD: Peter Briza

PROVIDER: PXD045513 | Pride | 2024-01-26

REPOSITORIES: Pride

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			Action	DRS
	PB8610.mgf	Mgf
	PB8610.raw	Raw
	PB8613.mgf	Mgf
	PB8613.raw	Raw
	PB8618.mgf	Mgf

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Publications

Ola1p trafficking indicates an interaction network between mitochondria, lipid droplets, and stress granules in times of stress.

Kovacs Melanie M Geltinger Florian F Schartel Lukas L Pöschl Simon S Briza Peter P Paschinger Manuel M Boros Kitti K Felder Thomas Klaus TK Wimmer Herbert H Duschl Jutta J Rinnerthaler Mark M

Journal of lipid research 20231109 12

Protein aggregates arise naturally under normal physiological conditions, but their formation is accelerated by age or stress-induced protein misfolding. When the stressful event dissolves, these aggregates are removed by mechanisms, such as aggrephagy, chaperone-mediated autophagy, refolding attempts, or the proteasome. It was recently shown that mitochondria in yeast cells may support these primarily cytosolic processes. Protein aggregates attach to mitochondria, and misfolded proteins are tra ...[more]

PMID: 37949369

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Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

Project description:Ola1 is implicated in various stress response pathways, as well as in cancer and tumor progression. However, Ola1p functions are divergent between species and still remain poorly understood. Here, we studied the role of Ola1p in the heat shock response in Saccharomyces cerevisiae. We show that deletion of OLA1 results in higher levels of proteins with protective functions for proteome stability under heat stress. We found that Ola1p enriches in detergent-resistant protein aggregates during heat stress. In heat-stressed yeast cells, it rapidly forms assemblies that localize to stress granules. In vitro, Ola1p assembly is protein autonomous and coincides with structural rearrangements that occur at similar temperatures and pH values seen in cells. We further observed that deletion of OLA1 leads to increased ubiquitination of protein aggregates formed during heat stress. Upon stress relief, central factors for protein refolding and the clearance of protein aggregates are synthesized in higher amounts in dola1 cells, whereas global translation reinitiation is decreased in these cells. Our data suggest that Ola1p is a positive factor for stabilizing the misfolded proteome that is sequestered in cytoplasmic stress granules during heat stress and, thereby, enables cells to efficiently restore a functional proteome after stress relief.

2022-02-17 | PXD026323 | Pride

Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

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Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

2022-02-17 | PXD025615 | Pride

Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

Project description:Ola1 is implicated in various stress response pathways, as well as in cancer and tumor progression. However, Ola1p functions are divergent between species and still remain poorly understood. Here, we studied the role of Ola1p in the heat shock response in Saccharomyces cerevisiae. We show that deletion of OLA1 results in higher levels of proteins with protective functions for proteome stability under heat stress. We found that Ola1p enriches in detergent-resistant protein aggregates during heat stress. In heat-stressed yeast cells, it rapidly forms assemblies that localize to stress granules. In vitro, Ola1p assembly is protein autonomous and coincides with structural rearrangements that occur at similar temperatures and pH values seen in cells. We further observed that deletion of OLA1 leads to increased ubiquitination of protein aggregates formed during heat stress. Upon stress relief, central factors for protein refolding and the clearance of protein aggregates are synthesized in higher amounts in ola1 cells, whereas global translation reinitiation is decreased in these cells. Our data suggest that Ola1p is a positive factor for stabilizing the misfolded proteome that is sequestered in cytoplasmic stress granules during heat stress and, thereby, enables cells to efficiently restore a functional proteome after stress relief.

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Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

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Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

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Optimization of codon translation rates via tRNA modifications maintains proteome integrity

Project description:Proteins begin to fold as they emerge from translating ribosomes. The kinetics of ribosome transit along a given mRNA can influence nascent chain folding, but the extent to which individual codon translation rates impact proteome integrity remains unknown. Here, we show that slower decoding of discrete codons elicits widespread protein aggregation in vivo. Using ribosome profiling, we find that loss of anticodon wobble uridine (U34) modifications in a subset of tRNAs leads to ribosome pausing at their cognate codons in S. cerevisiae and C. elegans. Yeast cells lacking U34 modifications exhibit gene expression hallmarks of proteotoxic stress and accumulate aggregates of endogenous proteins with key cellular functions. Moreover, these cells are severely compromised in clearing stress-induced protein aggregates. Overexpression of hypomodified tRNAs alleviates ribosome pausing, concomitantly restoring protein homeostasis. Our findings demonstrate that modified U34 is an evolutionarily conserved accelerator of decoding and reveal an unanticipated role for tRNA anticodon modifications in maintaining proteome integrity. Ribosome profiling of wild-type and tRNA modification-deficient yeast and nematodes. Yeast samples were generated in various growth conditions (rich medium versus stress induced by treatment with diamide or rapamycin) and paired mRNA-Seq was performed on a subset of samples. Dataset contains three biological replicates for yeast samples and two biological replicates for nematode samples.

2015-06-04 | E-GEOD-67387 | biostudies-arrayexpress

Distinct types of intramitochondrial protein aggregates protect mitochondria against proteotoxic stress - Data Set1: HSP78 AP-MS

Project description:Mitochondria consist of hundreds of proteins, most of which are long-lived and inaccessible to the proteasomal quality control system of the cytosol. How cells stabilize the mitochondrial proteome during challenging conditions is poorly understood. Here we show that mitochondria form spatially defined protein aggregates as a stress-protecting mechanism. Thereby different types of intramitochondrial protein aggregates can be distinguished. The mitoribosomal protein Var1 (uS3m) undergoes a stress-induced transition from a soluble, chaperone-stabilized protein that is prevalent under benign conditions to an insoluble aggregated form upon acute stress. The formation of Var1 bodies stabilizes mitochondrial proteostasis presumably by sequestration of aggregation-prone proteins. The AAA chaperone Hsp78 associates with a different type of intramitochondrial aggregate. These Hsp78-bound aggregates sequester non-native matrix proteins to promote their subsequent folding or Pim1-mediated degradation. Our study shows that mitochondrial proteins actively control the formation of different types of intramitochondrial protein aggregates which actively cooperate to stabilize the mitochondrial proteome during proteotoxic stress conditions.

2024-03-26 | PXD045196 | Pride

Distinct types of intramitochondrial protein aggregates protect mitochondria against proteotoxic stress - Data Set3: VAR1 AP-MS

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