Ubiquitinated proteasome inhibitor is a component of the 26 S proteasome complex.

Abstract:

:Western blot analysis, using a polyclonal antibody to the 240-kDa endogenous inhibitor of the 20 S proteasome, revealed that the inhibitor is a component of the 26 S complex. Although isolated inhibitor displayed a single 40-kDa band on SDS-PAGE, the antibody detected a 55-kDa component in the 26 S proteasome complex. Ubiquitin polyclonal antibody recognized the same 55-kDa component but did not react with free 40-kDa inhibitor subunit. Addition of purified 40-kDa inhibitor to a ubiquitin ligating system also generated the 55-kDa species. In crude erythrocyte extracts, most of the inhibitor migrated at 55 kDa in the presence of ATP but shifted to 40 kDa in the absence of ATP, consistent with removal of ubiquitin. It is suggested that ubiquitination of the inhibitor may be involved in regulating assembly and/or activity of the 26 S proteasome complex.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Li XS,Etlinger JD

doi

10.1021/bi00163a001

subject

Has Abstract

pub_date

1992-12-08 00:00:00

pages

11964-7

issue

48

eissn

0006-2960

issn

1520-4995

journal_volume

31

pub_type

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