Endoproteolytic Activity of the Proteasome

Overview

Journal Science

Specialty Science

Date 2002 Dec 14

PMID 12481023

Citations 155

Authors

Chang-Wei Liu

Michael J Corboy

George N DeMartino

Philip J Thomas

Affiliations

Soon will be listed here.

Abstract

The proteasome plays a central role in the degradation of regulatory and misfolded proteins. Current models suggest that substrates access the internal catalytic sites by processively threading their termini through the gated substrate channel. Here, we found that latent (closed) and activated (open) proteasomes degraded two natively disordered substrates at internal peptide bonds even when they lacked accessible termini, suggesting that these substrates themselves promoted gating of the proteasome. This endoproteolysis provides a molecular mechanism for regulated release of transcription factors from inactive precursors as well as a means of accessing internal folding defects of misfolded multidomain proteins.

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