Structures of chaperone-associated assembly intermediates reveal coordinated mechanisms of proteasome biogenesis.

ABSTRACT: The proteasome mediates most selective protein degradation. Proteolysis occurs within the 20S core particle (CP), a barrel-shaped chamber with an α₇β₇β₇α₇ configuration. CP biogenesis proceeds through an ordered multistep pathway requiring five chaperones, Pba1-4 and Ump1. Using Saccharomyces cerevisiae, we report high-resolution structures of CP assembly intermediates by cryogenic-electron microscopy. The first structure corresponds to the 13S particle, which consists of a complete α-ring, partial β-ring (β2-4), Ump1 and Pba1/2. The second structure contains two additional subunits (β5-6) and represents a later pre-15S intermediate. These structures reveal the architecture and positions of Ump1 and β2/β5 propeptides, with important implications

SUBMITTER: Schnell HM 

PROVIDER: S-EPMC8160580 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature