Charlotte Weiss

Introduction Click to copy section linkSection link copied! The degradation of proteins into peptides by the 26S proteasome plays a central role in proteostasis and the regulation of cellular pathways, including the immune response. (1,2) Proteolysis takes place inside the barrel-shaped 20S core of the proteasome, to which access is controlled by the 19S regulatory particle. (3,4) The small protein ubiquitin serves as the common signal for protein degradation.

Valuation of Samples Under the influence of MAS, soluble biomolecules are sedimented, i.e., they become immobilized in a dense phase on the walls of the MAS rotor. (40) To ensure a high filling factor, this process is usually initiated outside of the spectrometer in an ultracentrifuge, using a dedicated packing tool. (41) Because of its small size (42) (9.4 kDa, without isotopic labeling), it is not a priori clear that this sample preparation method is effective for the N-domain of FAT10.

Abstract Under inflammatory conditions, the ubiquitin-like modifier FAT10 targets proteins for rapid and irreversible degradation by the 26S proteasome. FAT10 is degraded along with its substrates and in this process, the loose folding of FAT10 and adapter protein NUB1L have long been suspected to play crucial roles. We report here the investigation of the N-domain of FAT10 and its interaction with NUB1L by magic-angle spinning (MAS) NMR spectroscopy.