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Critical elements in proteasome assembly

Nature Structural Biology volume 1, pages 765–770 (1994)Cite this article

Abstract

Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assembled and proteolytically active proteasomes. Post-translational processing of the β-subunit occurs in E. coli as it does in Thermoplasma. Coexpression of the α-subunit and the βΔpro-subunit, a mutant β-subunit lacking the propeptide, also yields fully assembled and active proteasomes. This indicates that the β-propeptide is not essential for the folding and assembly of Thermoplasma proteasomes. Separately expressed α-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 α-type proteins, is essential for assembly. In the absence of α-subunits the β-subunits are monomeric and post-translational processing of the β-propeptide does not occur.

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  1. Max-Planck-Institut für Biochemie, D-82152, Martinsried, Germany

    Peter Zwickl, Jörg Kleinz & Wolfgang Baumeister

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Zwickl, P., Kleinz, J. & Baumeister, W. Critical elements in proteasome assembly. Nat Struct Mol Biol 1, 765–770 (1994). https://doi.org/10.1038/nsb1194-765

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