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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis

Andrew R. Kusmierczyk1 / Mark Hochstrasser2

1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA

2Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA

Corresponding author

Citation Information: Biological Chemistry. Volume 389, Issue 9, Pages 1143–1151, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2008.130, August 2008

Publication History

Published Online:
2008-08-19

Abstract

The 26S proteasome is the key eukaryotic protease responsible for the degradation of intracellular proteins. Protein degradation by the 26S proteasome plays important roles in numerous cellular processes, including the cell cycle, differentiation, apoptosis, and the removal of damaged or misfolded proteins. How this 2.5-MDa complex, composed of at least 32 different polypeptides, is assembled in the first place is not well understood. However, it has become evident that this complicated task is facilitated by a framework of protein factors that chaperone the nascent proteasome through its various stages of assembly. We review here the known proteasome-specific assembly factors, most only recently discovered, and describe their potential roles in proteasome assembly, with an emphasis on the many remaining unanswered questions about this intricate process of assisted self-assembly.

Keywords: assembly factor; maturation; protein complex; yeast

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