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

Jonas Boehringer, Christiane Riedinger, Konstantinos Paraskevopoulos, Eachan O D Johnson, Edward D Lowe, Christina Khoudian, Dominique Smith, Martin E M Noble, Colin Gordon, Jane A Endicott

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)55-65
Number of pages11
JournalBiochemical Journal
Volume448
Issue number1
DOIs
Publication statusPublished - 15 Nov 2012

Keywords

  • Animals
  • Arabidopsis Proteins
  • Carrier Proteins
  • Circular Dichroism
  • Crystallography, X-Ray
  • Drosophila Proteins
  • Microtubule-Associated Proteins
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Peptide Fragments
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • Protein Conformation
  • Protein Interaction Mapping
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Structure-Activity Relationship
  • Ubiquitin
  • Winged-Helix Transcription Factors

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