| Abstrakt: |
Our studies showed that the living irradiated Saccharomyces cerevisiae has a good biosorption capacity for strontium and high tolerance to irradiation, but the mechanisms of this bioaccumulation are largely unknown. The mechanisms of S. cerevisiae to Sr2+ bioaccumulation was investigated using proteomics and metalloproteomics approaches. We previously identified 52 differentially expressed proteins (DEPs) by comparing the effect of Sr2+ adsorption on the proteome of S. cerevisiae. The selected DEPs were further analyzed using bioinformatics methods. A protein–protein interaction (PPI) network was constructed and analyzed using Search Tool for the Retrieval of Interacting Genes (STRING) and Cytoscape. Functional and signaling pathways of the identified DEPs with significant p-values were identified. We screened for the hub DEPs Ssa3p (SSA3), Kar2p (KAR2), Ssa4p (SSA4), Act1p (ACT1), Tubulin alpha chain (TUB1), Tubulin beta chain (TUB2), and ATP synthase subunit alpha (ATP1). The strontium-binding proteins of the living irradiated S. cerevisiae were purified by immobilized metal affinity chromatography and the cellular disposition and function of metals during the metabolism of S. cerevisiae were identified by liquid chromatography coupled with tandem mass spectrometry. Finally, 32 strontium-binding proteins were identified, and STRING was utilized to construct the PPI of the strontium-binding proteins and the selected hub DEPs, which were also analyzed using bioinformatics methods. Studies have shown that vacuolar transport, endosomal transport, and vesicle-mediated transport are critical to Sr2+ bioaccumulation, so we screened out that KAR2 is related to strontium detoxification, Sr2+ is transported into the cell through Rsn1p (RSN1), and ACT1 is related to strontium transport into the vacuole. [ABSTRACT FROM AUTHOR] |
