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Critical elements in proteasome assembly

Critical elements in proteasome assembly Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assembled and proteolytically active proteasomes. Post-translational processing of the β-subunit occurs in E. coli as it does in Thermoplasma. Coexpression of the α-subunit and the βΔpro-subunit, a mutant β-subunit lacking the propeptide, also yields fully assembled and active proteasomes. This indicates that the β-propeptide is not essential for the folding and assembly of Thermoplasma proteasomes. Separately expressed α-subunits assemble into heptameric rings indistinguishable from the terminal rings of a proteasome. Mutational analysis shows that the amino terminus, which is highly conserved in all proteasomal α-type proteins, is essential for assembly. In the absence of α-subunits the β-subunits are monomeric and post-translational processing of the β-propeptide does not occur. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Structural & Molecular Biology Springer Journals

Critical elements in proteasome assembly

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References (44)

Publisher
Springer Journals
Copyright
Copyright © 1994 by Nature Publishing Group
Subject
Life Sciences; Life Sciences, general; Biochemistry, general; Protein Structure; Membrane Biology; Biological Microscopy
ISSN
1545-9993
eISSN
1545-9985
DOI
10.1038/nsb1194-765
Publisher site
See Article on Publisher Site

Abstract

Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assembled and proteolytically active proteasomes. Post-translational processing of the β-subunit occurs in E. coli as it does in Thermoplasma. Coexpression of the α-subunit and the βΔpro-subunit, a mutant β-subunit lacking the propeptide, also yields fully assembled and active proteasomes. This indicates that the β-propeptide is not essential for the folding and assembly of Thermoplasma proteasomes. Separately expressed α-subunits assemble into heptameric rings indistinguishable from the terminal rings of a proteasome. Mutational analysis shows that the amino terminus, which is highly conserved in all proteasomal α-type proteins, is essential for assembly. In the absence of α-subunits the β-subunits are monomeric and post-translational processing of the β-propeptide does not occur.

Journal

Nature Structural & Molecular Biology – Springer Journals

Published: Nov 1, 1994

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