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A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

The proteasome consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP), which selects ubiquitinated substrates for translocation into the CP. An eight-subunit subcomplex of the RP, the lid, can be dissociated from proteasomes prepared from a deletion mutant for Rpn10, an RP subunit. A second subcomplex, the base, contains all six proteasomal ATPases and links the RP to the CP. The base is sufficient to activate the CP for degradation of peptides or a nonubiquitinated protein, whereas the lid is required for ubiquitin-dependent degradation. By electron microscopy, the base and the lid correspond to the proximal and distal masses of the RP, respectively. The lid subunits share sequence motifs with components of the COP9/signalosome complex and eIF3, suggesting that these functionally diverse particles have a common evolutionary ancestry.

Pubmed ID: 9741626

Authors

  • Glickman MH
  • Rubin DM
  • Coux O
  • Wefes I
  • Pfeifer G
  • Cjeka Z
  • Baumeister W
  • Fried VA
  • Finley D

Journal

Cell

Publication Data

September 4, 1998

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM43601

Mesh Terms

  • Carrier Proteins
  • Cysteine Endopeptidases
  • DNA-Binding Proteins
  • Fungal Proteins
  • Microscopy, Electron
  • Multienzyme Complexes
  • Multiprotein Complexes
  • Peptide Hydrolases
  • Plant Proteins
  • Proteasome Endopeptidase Complex
  • Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-ets
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Transcription Factors
  • Ubiquitins