Regulation of the 26 S Proteasome Complex During Oxidative Stress

• DOI: 10.1126/scisignal.2001232
• Publication Date: 2010-12-07T22:56:15Z
• Authors: Xiaorong Wang; James Yen; Peter Kaiser; Lan Huang
• Keywords: 0301 basic medicine; Proteasome Endopeptidase Complex; Saccharomyces cerevisiae Proteins; Dose-Response Relationship, Drug; Blotting, Western; Hydrogen Peroxide; Saccharomyces cerevisiae; Oxidants; Mass Spectrometry; Oxidative Stress; Protein Subunits; 03 medical and health sciences; HEK293 Cells; Mutation; Humans; Protein Binding; Transcription Factors

The proteasome plays a pivotal role in the cellular response to oxidative stress. Here, we used biochemical and mass spectrometric methods investigate structural changes 26S proteasomes from yeast mammalian cells exposed hydrogen peroxide (H₂O₂). Oxidative stress induced dissociation of 20S core particle 19S regulatory proteasome, which resulted loss activities accumulation ubiquitinated proteins. H₂O₂ triggered increased association proteasome-interacting protein Ecm29 with purified particle. Deletion ECM29 prevented disassembly stress, ecm29 mutants were more sensitive than wild-type cells, suggesting that separation particles is important for recovery amount free was required degrade oxidized Ecm29-dependent independent Yap1, transcription factor critical yeast, thus functions as parallel defense pathway against H₂O₂-induced