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Identification of ubiquitin-like protein-binding subunits of the 26S proteasome.

Abstract：

:Ubiquitin-like proteins Rad23 and Dsk2 have recently been shown to be capable of binding both polyubiquitin chains and the 26S proteasome. The ubiquitin-like domains (Ubls) of Rad23 and Dsk2 are indispensable for their interaction with the 26S proteasome, but the proteasome subunits capable of binding the Ubl have not been identified. Here, we report that the Ubls of both Rad23 and Dsk2 can bind with the 19S regulatory particle (RP) of the 26S proteasome in vivo and in vitro. A competition assay using the respective Ubls of Rad23 and Dsk2 revealed that they bind to the RP in a competitive manner. The base subcomplex of the RP was found to have the ability to bind the Ubl. By cross-linking experiments, Rpn1 and Rpn2 were identified as Ubl-binding subunits. Taken together, the results suggest that the Rpn1 and Rpn2 in the base subcomplex form the receptor for the ubiquitin-like protein.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Saeki Y,Sone T,Toh-e A,Yokosawa H

doi

10.1016/s0006-291x(02)02002-8

subject

Has Abstract

pub_date

2002-08-30 00:00:00

pages

813-9

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006291X02020028

journal_volume

296

pub_type

杂志文章

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