Expression data of FMN supplementation from Saccharomyces cerevisiae

Alzheimer's disease (AD) is hallmarked by progressive neurodegeneration. Aggregation of amyloid-ß peptides (Aß) is thought to play a pivotal role in driving AD pathogenesis, yet the underlying mechanisms remain unclear. Here, we use yeast genome-scale screening to study global synthetic genetic interactions and identify toxicity modifiers of Aß42. We find that the gene encoding riboflavin kinase (FMN1) and its metabolic product flavin mononucleotide (FMN) are connected to AD. These relationship between Aß42 and FMN was previously unknown. As a cofactor for flavoenzymes, FMN supplementation appears to attune many cellular processes to ameliorate Aß42 toxicity. RNA-seq analysis further confirms FMN's cytoprotective mechanisms. Our findings provide increased understanding of FMN regulated cellular pathways which are associated with potential targets for AD treatment. Overall design: The goal of the present study is to evaluate the impact of FMN supplementation on yeast strains. Saccharomyces cerevisiae expressing Aß42 peptide or control (only promoter and terminator sequences) was pre-grown overnight, diluted to an initial OD600nm of 0.1 in medium. 5mM of FMN (Riboflavin 5'-monophosphate sodium salt) were supplemented to culture for continuous treatment. Samples were taken from biological triplicate cultures during exponential phase (EX).