Molecular mechanisms of proteasome assembly

Nat Rev Mol Cell Biol. 2009 Feb;10(2):104-15. doi: 10.1038/nrm2630.


The 26S proteasome is a highly conserved protein degradation machine that consists of the 20S proteasome and 19S regulatory particles, which include 14 and 19 different polypeptides, respectively. How the proteasome components are assembled is a fundamental question towards understanding the process of protein degradation and its functions in diverse biological processes. Several proteasome-dedicated chaperones are involved in the efficient and correct assembly of the 20S proteasome. These chaperones help the initiation and progression of the assembly process by transiently associating with proteasome precursors. By contrast, little is known about the assembly of the 19S regulatory particles, but several hints have emerged.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Dimerization
  • Evolution, Molecular
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • Humans
  • Models, Molecular
  • Molecular Chaperones / metabolism
  • Proteasome Endopeptidase Complex* / chemistry
  • Proteasome Endopeptidase Complex* / genetics
  • Proteasome Endopeptidase Complex* / metabolism
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Subunits / metabolism*
  • Ubiquitin / metabolism


  • Archaeal Proteins
  • Bacterial Proteins
  • Fungal Proteins
  • Molecular Chaperones
  • Protein Subunits
  • Ubiquitin
  • Proteasome Endopeptidase Complex
  • 26S proteasome non-ATPase regulatory subunit 13