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Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation

Lookup NU author(s): Professor Martin Noble, Professor Jane Endicott

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Abstract

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.


Publication metadata

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

Year: 2012

Volume: 448

Issue: 1

Pages: 55-65

Print publication date: 20/08/2012

Date deposited: 04/01/2013

ISSN (print): 0264-6021

ISSN (electronic): 1470-8728

Publisher: Portland Press Ltd.

URL: http://dx.doi.org/10.1042/BJ20120542

DOI: 10.1042/BJ20120542


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