Dataset for suppressors of amyloid-β toxicity and their functions in recombinant protein production in yeast.

Chen X, Li X, Ji B, Wang Y, Ishchuk OP, Vorontsov E, Petranovic D, Siewers V, Engqvist MKM

Data Brief 42 (-) 108322 [2022-06-00; online 2022-05-27]

The production of recombinant proteins at high levels often induces stress-related phenotypes by protein misfolding or aggregation. These are similar to those of the yeast Alzheimer's disease (AD) model in which amyloid-β peptides (Aβ42) were accumulated [1], [2]. We have previously identified suppressors of Aβ42 cytotoxicity via the genome-wide synthetic genetic array (SGA) [3] and here we use them as metabolic engineering targets to evaluate their potentiality on recombinant protein production in yeast Saccharomyces cerevisiae. In order to investigate the mechanisms linking the genetic modifications to the improved recombinant protein production, we perform systems biology approaches (transcriptomics and proteomics) on the resulting strain and intermediate strains. The RNAseq data are preprocessed by the nf-core/RNAseq pipeline and analyzed using the Platform for Integrative Analysis of Omics (PIANO) package [4]. The quantitative proteome is analyzed on an Orbitrap Fusion Lumos mass spectrometer interfaced with an Easy-nLC1200 liquid chromatography (LC) system. LC-MS data files are processed by Proteome Discoverer version 2.4 with Mascot 2.5.1 as a database search engine. The original data presented in this work can be found in the research paper titled "Suppressors of Amyloid-β Toxicity Improve Recombinant Protein Production in yeast by Reducing Oxidative Stress and Tuning Cellular Metabolism", by Chen et al. [5].

Glycoproteomics and MS Proteomics [Service]

PubMed 35677454

DOI 10.1016/j.dib.2022.108322

Crossref 10.1016/j.dib.2022.108322

pmc: PMC9168475
pii: S2352-3409(22)00524-8