Abstract
Proteasomes are large (700 kDa) multisubunit proteinase complexes which form the catalytic core of 26S proteasomes (approx. 2,000 kDa) and which constitute the major non-lysosomal protein degradation machinery in eukaryotic cells [1]. Related proteinases with similar structures have been purified from some archaebacteria [2] and are also found in eubacteria [3]. 20S proteasomes have a hollow cylindrical structure with catalytic sites located inside the central cavity. They have a novel catalytic mechanism and require protein substrates to be readily unfolded for degradation to small peptides inside the cylindrical structure. Eukaryotic 20S proteasomes are complex particles composed of 14–17 different subunits of 22–34 kDa. They are found in the nucleus and in the cytoplasm and can account for up to 1% of the soluble cellular protein. Regulatory complexes bind to the ends of the cylinder giving rise to 26S proteasomes and other regulated complexes. The 26S proteasome is responsible for the recognition and degradation of proteins involved in cell cycle regulation, transcriptional regulation and signal transduction, in many cases by ubiquitin-dependent mechanisms. Proteasomes also play an important role in the processing of antigens for presentation of peptides by the major histo-compatibility complex (MHC) class I pathway.
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Rivett, A.J., Mason, G.G.F. (1999). Proteasomes. In: Turk, V. (eds) Proteases New Perspectives. MCBU Molecular and Cell Biology Updates. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8737-3_4
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DOI: https://doi.org/10.1007/978-3-0348-8737-3_4
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