Proteomics

Dataset Information

0

Insoluble fraction_Heat stress_S.pombe LC-MSMS


ABSTRACT: We have carried out proteomic studies to identify the thermo-unstable proteome fraction in fission yeast. We have performed biochemical separation of pellet fractions by centrifugation of whole cell extracts from wild-type cultures grown at different temperatures, and performed untagged liquid chromatography coupled to tandem MS (LC-MS/MS) of biological triplicates. We demonstrate that formation of protein aggregates during heat shock is a chaperone-mediated adaptation strategy which occurs with thermo-unstable endogenous proteins as well.

INSTRUMENT(S):

ORGANISM(S): Schizosaccharomyces Pombe 927

SUBMITTER: Susanna Boronat  

LAB HEAD: Elena Hidalgo

PROVIDER: PXD014400 | Pride | 2020-02-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2019MQ005_SUBO_001to009_XLtest.pdResult Other
2019MQ005_SUBO_30_1_1ug.raw Raw
2019MQ005_SUBO_30_2_1ug.raw Raw
2019MQ005_SUBO_30_3_1ug.raw Raw
2019MQ005_SUBO_37_1_1ug.raw Raw
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Publications

Chaperone-Facilitated Aggregation of Thermo-Sensitive Proteins Shields Them from Degradation during Heat Stress.

Cabrera Margarita M   Boronat Susanna S   Marte Luis L   Vega Montserrat M   Pérez Pilar P   Ayté José J   Hidalgo Elena E  

Cell reports 20200201 7


Cells have developed protein quality-control strategies to manage the accumulation of misfolded substrates during heat stress. Using a soluble reporter of misfolding in fission yeast, Rho1.C17R-GFP, we demonstrate that upon mild heat shock, the reporter collapses in protein aggregate centers (PACs). They contain and/or require several chaperones, such as Hsp104, Hsp16, and the Hsp40/70 couple Mas5/Ssa2. Stress granules do not assemble at mild temperatures and, therefore, are not required for PAC  ...[more]

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