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  Dissecting the assembly pathway of the 20s proteasome

Zühl, F., Seemüller, E., Golbik, R., & Baumeister, W. (1997). Dissecting the assembly pathway of the 20s proteasome. FEBS Letters, 418(1-2), 189-194.

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Zühl, F.1, Author              
Seemüller, E.1, Author              
Golbik, R., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Proteasome; Rhodococcus; Processing; Assembly; Propeptide.; Thermoplasma-acidophilum; Denatured subtilisin; Proteins; Expression.; Biochemistry & biophysics.
 Abstract: Proteasomes reach their mature active state via a complex cascade of folding, assembly and processing events, The Rhodococcus proteasome offers a means to dissect the assembly pathway and to characterize intermediates; its four subunits (alpha(1), alpha 2, beta 1, beta 2) assemble efficiently in vitro with any combination of alpha and beta. Assembly studies with wild-type and N-terminally truncated beta-subnnits in conjunction with refolding studies allowed to define the role of the propeptide,which is two-fold: It supports the initial folding of the beta-subunits and it promotes the maturation of the holoproteasomes. (C) 1997 Federation of European Biochemical Societies. [References: 23]

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 Dates: 1997-11-24
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 318716
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 418 (1-2) Sequence Number: - Start / End Page: 189 - 194 Identifier: -