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Updated: Jun 28, 2026
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
Published on: December 17, 2016
Protocol for the analysis of proteasome activity, assembly state, and composition in fission yeast extracts using
Gabriel Ruiz-Romero1, Rafael R Daga1, Silvia Salas-Pino1
1Centro Andaluz de Biología del Desarrollo, Universidad Pablo de Olavide, Departamento de Biología Molecular e Ingeniería Bioquímica, 41013 Carretera de Utrera, Seville, Spain.
Abstract:
The proteasome is a macromolecular complex responsible for degrading short-lived or damaged proteins. Proteasome analysis presents challenges due to its high molecular weight and low stability. Here, we present a protocol to assess proteasome activity, assembly, and composition in Schizosaccharomyces pombe. We describe steps for lysate preparation and native electrophoresis to separate proteasome complexes. We then detail procedures for detecting proteasome activity using fluorescent substrates, fluorescently-tagged native proteins, and non-tagged proteasome components by immunodetection in a single gel. For complete details on the use and execution of this protocol, please refer to Ruiz-Romero et al.1.
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