Sis1 potentiates the stress response to protein aggregation and elevated temperature
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA635137 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR11851375_1.fastq.gz | Fastqsanger.gz | |||
| SRR11851375_2.fastq.gz | Fastqsanger.gz | |||
| SRR11851376_1.fastq.gz | Fastqsanger.gz | |||
| SRR11851376_2.fastq.gz | Fastqsanger.gz | |||
| SRR11851377_1.fastq.gz | Fastqsanger.gz |
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Project description:Cells adapt to conditions that compromise protein conformational stability by activating various stress response pathways, but the mechanisms used in sensing misfolded proteins remain unclear. Moreover, aggregates of disease proteins often fail to induce a productive stress response. Here, using a yeast model of polyQ protein aggregation, we identified Sis1, an essential Hsp40 co-chaperone of Hsp70, as a critical sensor of proteotoxic stress. At elevated levels, Sis1 prevented the formation of dense polyQ inclusions and directed soluble polyQ oligomers towards the formation of permeable condensates. Hsp70 accumulated in a liquid-like state within this polyQ meshwork, resulting in a potent activation of the HSF1 dependent stress response. Sis1, and the homologous DnaJB6 in mammalian cells, also regulated the magnitude of the cellular heat stress response, suggesting a general role in sensing protein misfolding. Sis1/DnaJB6 functions as a limiting regulator to enable a dynamic stress response and avoid hypersensitivity to environmental changes.
2020-10-25 | GSE151215 | GEO
Project description:Cells adapt to conditions that compromise protein conformational stability by activating various stress response pathways, but the mechanisms used in sensing misfolded proteins remain unclear. Moreover, aggregates of disease proteins often fail to induce a productive stress response. Here, using a yeast model of polyQ protein aggregation, we identified Sis1, an essential Hsp40 co-chaperone of Hsp70, as a critical sensor of proteotoxic stress. At elevated levels, Sis1 prevented the formation of dense polyQ inclusions and directed soluble polyQ oligomers towards the formation of permeable condensates. Hsp70 accumulated in a liquid-like state within this polyQ meshwork, resulting in a potent activation of the HSF1 dependent stress response. Sis1, and the homologous DnaJB6 in mammalian cells, also regulated the magnitude of the cellular heat stress response, suggesting a general role in sensing protein misfolding. Sis1/DnaJB6 functions as a limiting regulator to enable a dynamic stress response and avoid hypersensitivity to environmental changes.
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Project description:denitrification and elevated temperature
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2012-11-18 | GSE14573 | GEO
Project description:Long-term exposure of Atlantic salmon to 19M-BM-0C resulted in cardiac gene and protein expression changes indicating that the unfolded protein response, vascularization, remodeling of connective tissue and altered innate immune responses were part of the cardiac acclimation or response to elevated temperature Heart tissue from Atlantic salmon (RNA poooled from N=3 fish per 3 replicate tanks) reared under normal (14 deg C) and elevated (19 deg C) temperatures were sampled after 21 (short-term) and 56 days (long-term acclimation), and gene expression changes between the elevated and the control temperature were assessed using microarray analysis.
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Project description:Long-term exposure of Atlantic salmon to 19°C resulted in cardiac gene and protein expression changes indicating that the unfolded protein response, vascularization, remodeling of connective tissue and altered innate immune responses were part of the cardiac acclimation or response to elevated temperature
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Project description:Morris2009 - α-Synuclein aggregation
variable temperature and pH
This model is described in the article:
Alpha-synuclein aggregation
variable temperature and variable pH kinetic data: a
re-analysis using the Finke-Watzky 2-step model of nucleation
and autocatalytic growth.
Morris AM, Finke RG.
Biophys. Chem. 2009 Mar; 140(1-3):
9-15
Abstract:
The aggregation of proteins is believed to be intimately
connected to many neurodegenerative disorders. We recently
reported an "Ockham's razor"/minimalistic approach to analyze
the kinetic data of protein aggregation using the Finke-Watzky
(F-W) 2-step model of nucleation (A-->B, rate constant k(1))
and autocatalytic growth (A+B-->2B, rate constant k(2)).
With that kinetic model we have analyzed 41 representative
protein aggregation data sets in two recent publications,
including amyloid beta, alpha-synuclein, polyglutamine, and
prion proteins (Morris, A. M., et al. (2008) Biochemistry 47,
2413-2427; Watzky, M. A., et al. (2008) Biochemistry 47,
10790-10800). Herein we use the F-W model to reanalyze protein
aggregation kinetic data obtained under the experimental
conditions of variable temperature or pH 2.0 to 8.5. We provide
the average nucleation (k(1)) and growth (k(2)) rate constants
and correlations with variable temperature or varying pH for
the protein alpha-synuclein. From the variable temperature
data, activation parameters DeltaG(double dagger),
DeltaH(double dagger), and DeltaS(double dagger) are provided
for nucleation and growth, and those values are compared to the
available parameters reported in the previous literature
determined using an empirical method. Our activation parameters
suggest that nucleation and growth are energetically similar
for alpha-synuclein aggregation (DeltaG(double
dagger)(nucleation)=23(3) kcal/mol; DeltaG(double
dagger)(growth)=22(1) kcal/mol at 37 degrees C). From the
variable pH data, the F-W analyses show a maximal k(1) value at
pH approximately 3, as well as minimal k(1) near the
isoelectric point (pI) of alpha-synuclein. Since solubility and
net charge are minimized at the pI, either or both of these
factors may be important in determining the kinetics of the
nucleation step. On the other hand, the k(2) values increase
with decreasing pH (i.e., do not appear to have a minimum or
maximum near the pI) which, when combined with the k(1) vs. pH
(and pI) data, suggest that solubility and charge are less
important factors for growth, and that charge is important in
the k(1), nucleation step of alpha-synuclein. The chemically
well-defined nucleation (k(1)) rate constants obtained from the
F-W analysis are, as expected, different than the 1/lag-time
empirical constants previously obtained. However, k(2)x[A](0)
(where k(2) is the rate constant for autocatalytic growth and
[A](0) is the initial protein concentration) is related to the
empirical constant, k(app) obtained previously. Overall, the
average nucleation and average growth rate constants for
alpha-synuclein aggregation as a function of pH and variable
temperature have been quantitated. Those values support the
previously suggested formation of a partially folded
intermediate that promotes aggregation under high temperature
or acidic conditions.
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BIOMD0000000566.
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2024-09-02 | BIOMD0000000566 | BioModels
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2012-03-20 | E-GEOD-34939 | biostudies-arrayexpress
Project description:Atlantic salmon production in Tasmania (Southern Australia) occurs near the upper limits of the species thermal tolerance. Summer water temperatures can average over 19°C over several weeks and have negative effects on performance and health. Liver tissue exerts important metabolic functions in thermal adaptation. With the aim of identifying the mechanisms underlying liver plasticity in response to chronic elevated temperature in Atlantic salmon, label-free quantitative shotgun proteomics was used to explore quantitative protein changes after 43 days of exposure to elevated temperature. A total of 277 proteins were differentially (adjusted p-value <0.05) expressed between the control (15°C) and elevated (21°C) temperature treatments. As predicted identified by Ingenuity pathway analysis (IPA), transcription and translation mechanisms, protein degradation via the proteasome, and cytoskeletal components were down-regulated at elevated temperature. In contrast, an up-regulated response was predicted identified for NRF2-mediated oxidative stress, endoplasmic reticulum stress, and amino acid degradation. The proteome response was paralleled by reduced fish condition factor and hepato-somatic index at elevated temperature . The present study provides further evidence of the interplay among different cellular machineries in a scenario of heat-induced energy deficit and oxidative stress, and refines present understanding of how Atlantic salmon cope with chronic exposure to temperature near the upper limits of thermal tolerance.
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