Proteomics

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Suppressors of amyloid-beta toxicity improve recombinant protein production by reducing oxidative stress and tunning cellular metabolism

ABSTRACT: In this study, we used a yeast Alzheimer’s disease model in which amyloid-β peptides (Aβ42) accumulate and induce stress-related phenotypes similar to overexpression of recombinant proteins. We validated that suppressors of Aβ42 cytotoxicity could reduce cell stress and improve recombinant protein production. Omics analyses and reverse metabolic engineering reveal potential regulatory hubs in cellular metabolism and protein synthesis, which may provide guidelines for engineering other cell factories for efficient protein production.

INSTRUMENT(S): Orbitrap Fusion Lumos

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

SUBMITTER: Egor Vorontsov  

LAB HEAD: Martin Engqvist

PROVIDER: PXD030111 | Pride | 2022-05-12

REPOSITORIES: Pride

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4124_ProteomeDiscoverere24.msf Msf
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Suppressors of amyloid-β toxicity improve recombinant protein production in yeast by reducing oxidative stress and tuning cellular metabolism.

Chen Xin X   Li Xiaowei X   Ji Boyang B   Wang Yanyan Y   Ishchuk Olena P OP   Vorontsov Egor E   Petranovic Dina D   Siewers Verena V   Engqvist Martin K M MKM  

Metabolic engineering 20220501

High-level production of recombinant proteins in industrial microorganisms is often limited by the formation of misfolded proteins or protein aggregates, which consequently induce cellular stress responses. We hypothesized that in a yeast Alzheimer's disease (AD) model overexpression of amyloid-β peptides (Aβ42), one of the main peptides relevant for AD pathologies, induces similar phenotypes of cellular stress. Using this humanized AD model, we previously identified suppressors of Aβ42 cytotoxi  ...[more]

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