hide
Free keywords:
Thermoplasma-acidophilum; Multicatalytic proteinase; Electron-microscopy; Groel; Expression; Complexes; Subunits; Lmp7; Rna.; Cell biology.
Abstract:
Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assembled and proteolytically active proteasomes. Posttranslational processing of the beta-subunit occurs in E. coli as it does in Thermoplasma. Coexpression of the alpha-subunit and the beta Delta pro-subunit, a mutant beta-subunit lacking the propeptide, also yields fully assembled and active proteasomes. This indicates that the beta-propeptide is not essential for the folding and assembly of Thermoplasma proteasomes, Separately expressed alpha-subunits assemble into heptameric rings indistinguishable from the terminal rings of a proteasome, Mutational analysis shows that the amino terminus, which is highly conserved in all proteasomal alpha-type proteins, is essential for assembly, In the absence of alpha-subunits the beta-subunits ave monomeric and post-translational processing of the beta-propeptide does not occur. [References: 40]
