Reconfiguration of the proteasome during chaperone-mediated assembly

摘要

蛋白酶体是一种降解“与泛素共轭的基质”的rn蛋白复合物。“26S蛋白酶体”由一个核心颗粒rn(CP)和由一个“底座”及一个“盖子”形成的rn一个调控颗粒(RP)组成。在这项研究中，rnDarliel Firfley及其同事提供了有关“底座一CP”rn复合物的组合体的结构和功能信息。%The proteasomal ATPase ring, comprising Rptl-Rpt6, associates with the heptameric o-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy- terminal tails inserting into pockets of the a-ring~(1-4). Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit~(5-10). Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP.