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



ID: 318377.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Subunit topology of the rhodococcus proteasome
Authors:Zühl, F.; Tamura, T.; Dolenc, I.; Cejka, Z.; Nagy, I.; Demot, R.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1997-01-02
Title of Journal:FEBS Letters
Volume:400
Issue / Number:1
Start Page:83
End Page:90
Audience:Not Specified
Abstract / Description:The 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis strain NI86/21, is built from two alpha-type and two beta-type subunits. In order to probe the subunit topology, we have set up an expression system which allows coexpression of the genes encoding the alpha- and beta-subunits in all. possible combinations. The four respective constructs obtained yielded fully assembled and proteolytically active proteasomes. Biochemical, kinetic and electron microscopy analysis allow us to rule out several of the models which were originally envisaged for the subunit topology of the Rhodococcus proteasome. The experiments further indicate that the assembly pathways of the Rhodococcus and of the Thermoplasma proteasome differ in some important details. [References: 30]
Free Keywords:Proteasome; Proteolysis; Rhodococcus; Gene expression.; Multicatalytic proteinase prosome; Thermoplasma-acidophilum; Structural features; Electrophoresis; Complex; Images.; 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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