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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318716.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Dissecting the assembly pathway of the 20s proteasome
Authors:Zühl, F.; Seemüller, E.; Golbik, R.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1997-11-24
Title of Journal:FEBS Letters
Volume:418
Issue / Number:1-2
Start Page:189
End Page:194
Audience:Not Specified
Abstract / Description:Proteasomes reach their mature active state via a complex cascade of folding, assembly and processing events, The Rhodococcus proteasome offers a means to dissect the assembly pathway and to characterize intermediates; its four subunits (alpha(1), alpha 2, beta 1, beta 2) assemble efficiently in vitro with any combination of alpha and beta. Assembly studies with wild-type and N-terminally truncated beta-subnnits in conjunction with refolding studies allowed to define the role of the propeptide,which is two-fold: It supports the initial folding of the beta-subunits and it promotes the maturation of the holoproteasomes. (C) 1997 Federation of European Biochemical Societies. [References: 23]
Free Keywords:Proteasome; Rhodococcus; Processing; Assembly; Propeptide.; Thermoplasma-acidophilum; Denatured subtilisin; Proteins; Expression.; Biochemistry & biophysics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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