RRC ID 46973
Author Saeki Y, Toh-E A, Kudo T, Kawamura H, Tanaka K.
Title Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle.
Journal Cell
Abstract The 26S proteasome is a highly conserved multisubunit protease that degrades ubiquitinated proteins in eukaryotic cells. The 26S proteasome consists of the proteolytic core particle (CP) and one or two 19S regulatory particles (RPs). Although the mechanisms of CP assembly are well described, the mechanism of RP assembly is largely unknown. Here, we show that four proteasome-interacting proteins (PIPs), Nas2/p27, Nas6/gankyrin, Rpn14/PAAF1, and Hsm3/S5b, bind specific Rpt subunits of the RP and interact each other genetically. Lack of these PIPs resulted in defective assembly of the 26S proteasome at an early stage, suggesting that these proteins are bona fide RP chaperones. Each of the RP chaperones formed distinct specific subassemblies of the base components and escorted them to mature RPs. Our results indicate that the RP assembly is a highly organized and elaborate process orchestrated by multiple proteasome-dedicated chaperones.
Volume 137(5)
Pages 900-13
Published 2009-5-29
DOI 10.1016/j.cell.2009.05.005
PII S0092-8674(09)00528-5
PMID 19446323
MeSH Humans Molecular Chaperones / metabolism Proteasome Endopeptidase Complex / metabolism* Proto-Oncogene Proteins / metabolism Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae Proteins / metabolism
IF 38.637
Times Cited 116
Pathogenic microorganisms ?