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  Thermoplasma acidophilum proteasomes degrade partially unfolded and ubiquitin-associated proteins

Wenzel, T., & Baumeister, W. (1993). Thermoplasma acidophilum proteasomes degrade partially unfolded and ubiquitin-associated proteins. FEBS Letters., 326(1-3), 215-218.

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Wenzel, T., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Chromatography, High Pressure Liquid; *Cysteine Endopeptidases/me [Metabolism]; Hemoglobin A/me [Metabolism]; Human; Hydrogen Peroxide/pd [Pharmacology]; Lactalbumin/me [Metabolism]; *Multienzyme Complexes/me [Metabolism]; Phenylhydrazines/pd [Pharmacology]; Protein Folding; *Proteins/me [Metabolism]; Substrate Specificity; *Thermoplasma/en [Enzymology]; *Ubiquitins/me [Metabolism]; Ubiquitins/pd [Pharmacology]
 Abstract: It is shown that proteasomes from the arachaebacterium Thermoplasma acidophilum selectively degrade substrate proteins partially unfolded by phenylhydrazine- or hydrogen peroxide-treatment. Surprisingly, the pre-incubation of the substrate proteins with ubiquitin is also sufficient to render them susceptible to proteolytic degradation by proteasomes. We propose that, upon spontaneously associating with the substrate protein, ubiquitin exerts a chaotropic effect on it; this may involve the exposure of hydrophobic segments of the polypeptide chain which are recognized by the binding sites of the proteasome.

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 Dates: 1993
 Publication Status: Published in print
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 Identifiers: eDoc: 318694
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Title: FEBS Letters.
Source Genre: Journal
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Pages: - Volume / Issue: 326 (1-3) Sequence Number: - Start / End Page: 215 - 218 Identifier: -