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  The 26S proteasome: A molecular machine designed for controlled proteolysis

Voges, D., Zwickl, P., & Baumeister, W. (1999). The 26S proteasome: A molecular machine designed for controlled proteolysis. Annual Review of Biochemistry, 68, 1015-1068.

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Genre: Journal Article
Alternative Title : Annu. Rev. Biochem

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Voges, D.1, Author              
Zwickl, P.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Protein degradation; Ubiquitin; Core complex; Regulatory complex.; Carboxyl-terminal hydrolase; Multicatalytic proteinase complex; Major-histocompatibility-complex; Tat-binding-protein; Multiubiquitin-chain-binding; Complete genome sequence; Mhc class-i; Ubiquitin-carrier protein; Non-atpase subunit; Nf-kappa-b.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built from similar to 31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. The regulatory complexes are also implicated in unfolding and translocation of ubiquitinated targets into the interior of the 20S complex, where they are degraded to oligopeptides. Structure, assembly and enzymatic mechanism of the 20S complex have been elucidated, but the functional organization of the 19S complex is less well understood. Most subunits of the 19S complex have been identified, however, specific functions have been assigned to only a few. A low-resolution structure of the 26S proteasome has been obtained by electron microscopy, but the precise arrangement of subunits in the 19S complex is unclear. [References: 412]

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 Dates: 1999
 Publication Status: Published in print
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 Identifiers: eDoc: 318446
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Title: Annual Review of Biochemistry
  Alternative Title : Annu. Rev. Biochem
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 68 Sequence Number: - Start / End Page: 1015 - 1068 Identifier: -