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Lookup NU author(s): Professor Martin Noble,
Professor Jane Endicott
The ubiquitin-proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. In the present paper we report the crystal structure of Rpn12, a proteasomal PCI-domain-containing protein. The structure helps to define a core structural motif for the PCI domain and identifies potential sites through which Rpn12 might form protein-protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vitro and reduces Rpn10 incorporation into proteasomes in vivo.
Author(s): Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EOD, Lowe ED, Khoudian C, Smith D, Noble MEM, Gordon C, Endicott JA
Publication type: Article
Publication status: Published
Journal: Biochemical Journal
Print publication date: 20/08/2012
Date deposited: 04/01/2013
ISSN (print): 0264-6021
ISSN (electronic): 1470-8728
Publisher: Portland Press Ltd.
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