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Journal Article

Critical elements in proteasome assembly

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Zwickl, P., Kleinz, J., & Baumeister, W. (1994). Critical elements in proteasome assembly. Nature Structural Biology, 1(11), 765-770.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-7377-8
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]