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The base of the proteasome regulatory particle exhibits chaperone-like activity.

Abstract：

:Protein substrates of the proteasome must apparently be unfolded and translocated through a narrow channel to gain access to the proteolytic active sites of the enzyme. Protein folding in vivo is mediated by molecular chaperones. Here, to test for chaperone activity of the proteasome, we assay the reactivation of denatured citrate synthase. Both human and yeast proteasomes stimulate the recovery of the native structure of citrate synthase. We map this chaperone-like activity to the base of the regulatory particle of the proteasome, that is, to the ATPase-containing assembly located at the substrate-entry ports of the channel. Denatured but not native citrate synthase is bound by the base complex. Ubiquitination of citrate synthase is not required for its binding or refolding by the base complex of the proteasome. These data suggest a model in which ubiquitin-protein conjugates are initially tethered to the proteasome by specific recognition of their ubiquitin chains; this step is followed by a nonspecific interaction between the base and the target protein, which promotes substrate unfolding and translocation.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Braun BC,Glickman M,Kraft R,Dahlmann B,Kloetzel PM,Finley D,Schmidt M

doi

10.1038/12043

keywords:

subject

Has Abstract

pub_date

1999-08-01 00:00:00

pages

221-6

issue

4

eissn

1465-7392

issn

1476-4679

journal_volume

1

pub_type

杂志文章

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