Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-6931
Main Title: A single α helix drives extensive remodeling of the proteasome lid and completion of regulatory particle assembly
Author(s): Tomko, Robert J.
Taylor, David W.
Chen, Zhuo A.
Wang, Hong-Wei
Rappsilber, Juri
Hochstrasser, Mark
Type: Article
Language Code: en
Abstract: Most short-lived eukaryotic proteins are degraded by the proteasome. A proteolytic core particle (CP) capped by regulatory particles (RPs) constitutes the 26S proteasome complex. RP biogenesis culminates with the joining of two large subcomplexes, the lid and base. In yeast and mammals, the lid appears to assemble completely before attaching to the base, but how this hierarchical assembly is enforced has remained unclear. Using biochemical reconstitutions, quantitative cross-linking/mass spectrometry, and electron microscopy, we resolve the mechanistic basis for the linkage between lid biogenesis and lid-base joining. Assimilation of the final lid subunit, Rpn12, triggers a large-scale conformational remodeling of the nascent lid that drives RP assembly, in part by relieving steric clash with the base. Surprisingly, this remodeling is triggered by a single Rpn12 α helix. Such assembly-coupled conformational switching is reminiscent of viral particle maturation and may represent a commonly used mechanism to enforce hierarchical assembly in multisubunit complexes.
URI: https://depositonce.tu-berlin.de//handle/11303/7753
http://dx.doi.org/10.14279/depositonce-6931
Issue Date: 2015
Date Available: 7-May-2018
DDC Class: 570 Biowissenschaften; Biologie
Subject(s): proteasome lid
regulatory particle assembly
RP assembly
rpn12 subunit
License: https://creativecommons.org/licenses/by/4.0/
Journal Title: Cell
Publisher: Cell Press
Publisher Place: Cambridge
Volume: 163
Issue: 2
Publisher DOI: 10.1016/j.cell.2015.09.022
Page Start: 432
Page End: 444
ISSN: 0092-8674
Appears in Collections:FG Bioanalytik » Publications

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