Rapid isolation and characterization of the yeast proteasome regulatory complex

被引：37

作者：

Saeki, Y

Toh-e, A

Yokosawa, H ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biochem, Sapporo, Hokkaido 0600812, Japan

[2] Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Genet Lab,Bunkyo Ku, Tokyo 1130033, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 273卷 / 02期

关键词：

26S proteasome; 19S regulatory complex; lid complex; base complex; multiubiquitin chain binding; immunoaffinity chromatography; yeast;

D O I：

10.1006/bbrc.2000.2980

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The 26S proteasome, which catalyzes degradation of ubiquitinated proteins, is composed of the 20S proteasome and the 19S complex. Recently, it has been reported that the 26S complex can be dissociated into the lid complex and the 20S-proteasome-base complex in a mutant yeast and that the lid complex is required for ubiquitin-dependent proteolysis. In the present study, we established methods for rapid isolation of the 19S complex, the lid complex, and the base complex from wild-type yeast. The isolated 19S complex was capable of binding to the 20S proteasome to reconstitute the 26S proteasome. In contrast with the previously reported result showing that Rpn10, a multiubiquitin chain binding subunit, is a component of the base complex, we present evidence that the lid complex isolated from wild-type yeast contains Rpn10. (C) 2000 Academic Press.

引用

页码：509 / 515

页数：7