Conserved proline residues in the coiled coil-OB domain linkers of Rpt proteins facilitate eukaryotic proteasome base assembly.

ABSTRACT: The proteasome is a large protease complex that degrades many different cellular proteins. In eukaryotes, the 26S proteasome contains six different subunits of the ATPases associated with diverse cellular activities family, Rpt1-Rpt6, which form a hexameric ring as part of the base subcomplex that drives unfolding and translocation of substrates into the proteasome core. Archaeal proteasomes contain only a single Rpt-like ATPases associated with diverse cellular activities ATPase, the proteasome-activating nucleotidase, which forms a trimer of dimers. A key proteasome-activating nucleotidase proline residue (P91) forms cis- and trans-peptide bonds in successive subunits around the ring, allowing efficient dimerization through upstream coiled coils. However, the importance of the equivalent

SUBMITTER: Cheng CL 

PROVIDER: S-EPMC8134078 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature