Prohibitin cross-linked aided interactome in yeast

The mitochondrial oxidative phosphorylation system (OXPHOS) contains subunits of dual genetic origin, namely the nuclear and the mitochondrial genome. Mounting the different subunits into functional OXPHOS complexes is aided by dedicated chaperones termed assembly factors. How unfunctional or superfluous proteins are recognized during assembly and directed to degradation is currently not understood. Here, we reveal that protein quality control is an integral part of assembly, which is organized in dedicated hubs gathering mitochondrial translation, protein import, assembly, and protein turnover. Fate-decision of newly synthesized proteins is achieved by molecular triaging engaging the evolutionary conserved prohibitin/m-AAA protease supercomplex and assembly chaperones. The localization of these competing activities in vicinity to the mitoribosomal tunnel exit allows for a rapid decision whether newly synthesized proteins are fed into OXPHOS assembly or to degradation. In total, three projects are hosted in this repository. 1) Phb1-Alfa DSG cross-linked immunoprecipitation 2) Metabolic switch from Glycerol to Glucose followed by Phb1-ALFA DSG cross-linked immunoprecipitation. 3) Phb2-ALFA DSG cross-linked immunoprecipitation.