Endoproteolytic activity of the proteasome

Chang Wei Liu, Michael J. Corboy, George N. DeMartino, Philip J. Thomas

Research output: Contribution to journalArticle

310 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)408-411
Number of pages4
JournalScience
Volume299
Issue number5605
DOIs
StatePublished - Jan 17 2003

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Proteasome Endopeptidase Complex
Catalytic Domain
Proteins
Transcription Factors
Peptides

ASJC Scopus subject areas

  • General

Cite this

Endoproteolytic activity of the proteasome. / Liu, Chang Wei; Corboy, Michael J.; DeMartino, George N.; Thomas, Philip J.

In: Science, Vol. 299, No. 5605, 17.01.2003, p. 408-411.

Research output: Contribution to journalArticle

Liu, Chang Wei ; Corboy, Michael J. ; DeMartino, George N. ; Thomas, Philip J. / Endoproteolytic activity of the proteasome. In: Science. 2003 ; Vol. 299, No. 5605. pp. 408-411.
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