title: Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome).
abstract: There have been many reports that eukaryotic cells contain ring-shaped 19S or 20S particles which are composed of numerous polypeptide subunits ranging in size between 25 and 35 kilodaltons. Because these particles seemed to copurify with inactive mRNA, they were assumed to function in regulating mRNA translation and hence were named 'prosomes' (for 'programmed-o-some'). A number of properties have been reported for these structures, including an association with specific RNA species or with certain heat-shock proteins and involvement in tRNA processing or aminoacyl tRNA synthesis. However, these proposed activities have not been supported by definitive evidence. During studies of the proteolytic systems in mammalian tissues, we noted many similarities between these 19S particles and the high molecular weight protease complexes that are present in most or all eukaryotic cells. This (700 kilodalton) enzyme complex, designated here as LAMP for 'large alkaline multi-functional protease', contains three distinct endoproteolytic sites which function at neutral or alkaline pH and are specific for hydrolysis of proteins, hydrophobic peptides, or basic peptides. This protease also exists in a latent form which can be activated by polylysine, fatty acids, or ATP. In this report, we show that the prosomes and these protease complexes are very similar or identical with respect to their size, polypeptide composition, immunological cross-reactivity, appearance in the electron microscope, radial symmetry of subunits, subcellular localization, and proteolytic activities. Therefore, the 'prosome' probably plays a critical role in intracellular protein breakdown, and we propose that it be renamed 'proteasome'.
authors.affiliation: Cold Spring Harbor Laboratory, New York 11724.
authors.forename: A P
authors.initials: AP
authors.lastname: Arrigo
authors.forename: K
authors.initials: K
authors.lastname: Tanaka
authors.forename: A L
authors.initials: AL
authors.lastname: Goldberg
authors.forename: W J
authors.initials: WJ
authors.lastname: Welch
mesh_terms: D000818:Animals; D002477:Cells / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D004586:Electrophoresis; D005057:Eukaryotic Cells / Q000201:enzymology*; D006367:HeLa Cells / Q000201:enzymology; D007425:Intracellular Membranes / Q000201:enzymology; D046911:Macromolecular Substances / Q000378:metabolism; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D012377:Rodentia
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D010447:Peptide Hydrolases