作为19S调节复合体装配平台的20S蛋白酶体。

The 20S proteasome as an assembly platform for the 19S regulatory complex.

作者信息

Hendil Klavs B, Kriegenburg Franziska, Tanaka Keiji, Murata Shigeo, Lauridsen Anne-Marie B, Johnsen Anders H, Hartmann-Petersen Rasmus

机构信息

Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.

出版信息

J Mol Biol. 2009 Nov 27;394(2):320-8. doi: 10.1016/j.jmb.2009.09.038. Epub 2009 Sep 23.

DOI:10.1016/j.jmb.2009.09.038

PMID:19781552

Abstract

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.

摘要

26S蛋白酶体由圆柱形的20S蛋白酶体组成，其两端附着有19S调节复合物。用高浓度盐处理会使调节复合物分离成两个亚复合物，即与20S蛋白酶体接触的基部和作为19S复合物远端部分的盖子。在此，我们描述了人类调节复合物的两种组装中间体。一种是两个ATP酶亚基Rpt3和Rpt6的二聚体。另一种是新生的Rpn2、Rpn10、Rpn11、Rpn13和Txnl1与预先存在的20S蛋白酶体相连形成的复合物。这种早期组装复合物尚未包含Rpn1或基部的任何ATP酶亚基。因此，19S调节复合物在预先存在的20S蛋白酶体上组装，并且盖子的一部分在基部之前组装。