Biogenesis of eukaryotic 20S proteasomes: The complex maturation pathway of a complex enzyme

Marion Schmidt, Peter M. Kloetzel

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


Eukaryotic 20S proteasomes harbor a remarkably complex architecture and unique proteolytic properties. Its catalytic mechanism places this enzyme in a new kind of protease family. The recently solved crystal structure of the yeast 20S complex, along with elucidation of the maturation pathway of human proteasomes, has allowed insight into structure/function relationships. Although not all of the unusual enzymatic properties such as broad substrate specificity, predominant generation of peptides with a specific size, or susceptibility to activating complexes can be explained in detail, knowledge of the structure provides important hints for an explanation of underlying mechanisms. Except for ribosome biogenesis, the complexity of eukaryotic proteasome maturation is without precedence. It is a slow process that involves a series of precisely ordered events. Proteasome structure formation is characterized by an initial cooperative formation of an α ring matrix, providing docking sites for a defined subset of β subunits. Subsequent structural rearrangement allows the residual subunits to bind, followed by dimerization of two half-proteasomes. The prosequences of β subunits exert specific functions during this process and are removed by cis- and trans- autocatalysis, most likely in the completely assembled proteasome of cylinder.

Original languageEnglish (US)
Pages (from-to)1235-1243
Number of pages9
JournalFASEB Journal
Issue number14
StatePublished - 1997
Externally publishedYes


  • Catalytic mechanism
  • Circular assemblies
  • Crystal structure
  • Proteasome maturation

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


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