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  Critical elements in proteasome assembly

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

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Zwickl, P.1, Autor           
Kleinz, J., Autor
Baumeister, W.1, Autor           
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1External Organizations, ou_persistent22              

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Schlagwörter: Thermoplasma-acidophilum; Multicatalytic proteinase; Electron-microscopy; Groel; Expression; Complexes; Subunits; Lmp7; Rna.; Cell biology.
 Zusammenfassung: 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]

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 Datum: 1994-11
 Publikationsstatus: Erschienen
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 Identifikatoren: eDoc: 318520
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Titel: Nature Structural Biology
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 1 (11) Artikelnummer: - Start- / Endseite: 765 - 770 Identifikator: -