The 20S Proteasome as an Assembly Platform for the 19S Regulatory Complex

被引：51

作者：

Hendil, Klavs B. ^{[1
]}

Kriegenburg, Franziska ^{[1
]}

Tanaka, Keiji ^{[2
]}

Murata, Shigeo ^{[3
]}

Lauridsen, Anne-Marie B. ^{[1
]}

Johnsen, Anders H. ^{[4
]}

Hartmann-Petersen, Rasmus ^{[1
]}

机构：

[1] Univ Copenhagen, Dept Biol, DK-2200 Copenhagen N, Denmark

[2] Tokyo Metropolitan Inst Med Sci, Lab Frontier Sci, Core Technol & Res Ctr, Setagaya Ku, Tokyo 1568506, Japan

[3] Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyou Ku, Tokyo 1130033, Japan

[4] Copenhagen Univ Hosp, Dept Clin Biochem, DK-2100 Copenhagen O, Denmark

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2009年 / 394卷 / 02期

关键词：

ubiquitin; proteasome; protein assembly; degradation; AAA; SACCHAROMYCES-CEREVISIAE; DEUBIQUITINATING ENZYME; SUBUNIT INTERACTIONS; 26S PROTEASOME; PROTEIN; PARTICLE; PATHWAY; YEAST; UBIQUITIN; SUBCOMPLEX;

D O I：

10.1016/j.jmb.2009.09.038

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

26S proteasomes consist of cylindrical 20S proteasomes with 19S regulatory complexes attached to the ends. Treatment with high concentrations of salt causes the regulatory complexes to separate into two sub-complexes, the base, which is in contact with the 20S proteasome, and the lid, which is the distal part of the 19S complex. Here, we describe two assembly intermediates of the human regulatory complex. One is a dimer of the two ATPase subunits, Rpt3 and Rpt6. The other is a complex of nascent Rpn2, Rpn10, Rpn11, Rpn13, and Txnl1, attached to preexisting 20S proteasomes. This early assembly complex does not yet contain Rpn1 or any of the ATPase subunits of the base. Thus, assembly of 19S regulatory complexes takes place on preexisting 20S proteasomes, and part of the lid is assembled before the base. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：320 / 328

页数：9

共 48 条

[1]

Thioredoxin Txnl1/TRP32 Is a Redox-active Cofactor of the 26 S Proteasome [J].