Reference - PMID:22906049 - Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation.
Reference summary
- PubMed ID
- PMID:22906049
- Title
- Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation.
- Authors
- Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA
- Citation
- Biochem J 2012 Nov 15;448(1):55-65
- Publication year
- 2012
- 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.
