The 26S proteasome: subunits and functions
- 1 January 1997
- journal article
- review article
- Published by Springer Nature in Molecular Biology Reports
- Vol. 24 (1/2) , 3-11
- https://doi.org/10.1023/a:1006876904158
Abstract
The 26S proteasome is an eukaryotic ATP-dependent, dumbbell-shaped protease complex with a molecular mass of approximately 2000 kDa. It consists of a central 20S proteasome, functioning as a catalytic machine, and two large V-shaped terminal modules, having possible regulatory roles, composed of multiple subunits of 25–110 kDa attached to the central portion in opposite orientations. The primary structures of all the subunits of mammalian and yeast 20S proteasomes have been determined by recombinant DNA techniques, but structural analyses of the regulatory subunits of the 26S proteasome are still in progress. The regulatory subunits are classified into two subgroups, a subgroup of at least 6 ATPases that constitute a unique multi-gene family encoding homologous polypeptides conserved during evolution and a subgroup of approximately 15 non-ATPase subunits, most of which are structurally unrelated to each other.Keywords
This publication has 34 references indexed in Scilit:
- cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein familyFEBS Letters, 1996
- ANTIGEN PROCESSING AND PRESENTATION BY THE CLASS I MAJOR HISTOCOMPATIBILITY COMPLEXAnnual Review of Immunology, 1996
- Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S proteaseFEBS Letters, 1996
- cDNA Cloning of p40, a Regulatory Subunit of the Human 26S Proteasome, and a Homolog of the Mov-34 Gene ProductBiochemical and Biophysical Research Communications, 1995
- cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1pFEBS Letters, 1995
- Subunits of the regulatory complex of the 26S proteaseMolecular Biology Reports, 1995
- Molecular biology of proteasomesMolecular Biology Reports, 1995
- Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteinsCurrent Biology, 1994
- The murine Mov-34 gene: Full-length cDNA and genomic organizationGenomics, 1991
- Molecular organization of a high molecular weight multi-protease complex from rat liverJournal of Molecular Biology, 1988