RRC ID 47483
著者 Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA.
タイトル Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation.
ジャーナル Biochem J
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.
巻・号 448(1)
ページ 55-65
公開日 2012-11-15
DOI 10.1042/BJ20120542
PII BJ20120542
PMID 22906049
PMC PMC3481250
MeSH Animals Arabidopsis Proteins / chemistry COP9 Signalosome Complex Carrier Proteins / chemistry Carrier Proteins / metabolism* Circular Dichroism Crystallography, X-Ray Drosophila Proteins / chemistry Microtubule-Associated Proteins / chemistry Models, Molecular Mutagenesis, Site-Directed Peptide Fragments / chemistry Peptide Fragments / metabolism Proteasome Endopeptidase Complex / metabolism* Protein Binding Protein Conformation Protein Interaction Mapping Protein Structure, Tertiary RNA-Binding Proteins Recombinant Proteins / metabolism Schizosaccharomyces / genetics Schizosaccharomyces / metabolism Schizosaccharomyces pombe Proteins / chemistry* Schizosaccharomyces pombe Proteins / genetics Schizosaccharomyces pombe Proteins / metabolism* Structure-Activity Relationship Ubiquitin / metabolism Winged-Helix Transcription Factors / chemistry
IF 4.097
引用数 14
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
遺伝子材料 pDUAL (RDB06178)