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Yeast response to protein misfolding induced by azetidine-2-carboxylic acid (AZC)

ABSTRACT: To identify proteins that interact with the yeast Tsa1 peroxiredoxin, we utilized an N-terminal Myc-tagged version of Tsa1 with a mutation in its resolving cysteineresidue (Tsa1-C171S) to trap and detect redox-dependent interactions. Yeast cells were left untreated, or treated with AZC or hydrogen peroxide prior to immunoprecipitation and mass spectrometry used to identify co-immunoprecipitating proteins.

INSTRUMENT(S): LTQ Orbitrap Velos

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

SUBMITTER: Chris Grant

LAB HEAD: Chris Grant

PROVIDER: PXD023668 | Pride | 2021-09-10

REPOSITORIES: Pride

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Tolerance to nascent protein misfolding stress requires fine-tuning of the cAMP/PKA pathway.

Kritsiligkou Paraskevi P Nowicki-Osuch Karol K Carter Zorana Z Kershaw Chris J CJ Creamer Declan R DR Weids Alan J AJ Grant Chris M CM

The Journal of biological chemistry 20210101

Protein aggregation is the abnormal association of misfolded proteins into larger, often insoluble structures that can be toxic during aging and in protein aggregation-associated diseases. Previous research has established a role for the cytosolic Tsa1 peroxiredoxin in responding to protein misfolding stress. Tsa1 is also known to downregulate the cAMP/protein kinase A (PKA) pathway as part of the response to hydrogen peroxide stress. However, whether the cAMP/PKA pathway is involved in protein ...[more]

PMID: 33894203

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