20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated

The 20 S proteasome core purified from Saccharomyces cerevisiae is inhibited by reduced glutathione (GSH), cysteine (Cys), or the GSH precursor gamma-glutamylcysteine. Chymotrypsin-like activity was more affected by GSH than trypsin-like activity, whereas the peptidylglutamyl-hydrolyzing activity (c...

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Veröffentlicht in:	The Journal of biological chemistry 2003-01, Vol.278 (1), p.679-685
Hauptverfasser:	Demasi, Marilene, Silva, Gustavo Monteiro, Netto, Luis Eduardo Soares
Format:	Artikel
Sprache:	eng
Schlagworte:	Bridged Bicyclo Compounds - metabolism Cell Survival Chelating Agents - metabolism Cysteine - chemistry Cysteine - metabolism Cysteine Endopeptidases - metabolism Dithiothreitol - metabolism Fluorescent Dyes - metabolism Glutathione - chemistry Glutathione - metabolism Hydrogen Peroxide - metabolism Multienzyme Complexes - metabolism Oxidants - metabolism Oxidation-Reduction Pentetic Acid - metabolism Proteasome Endopeptidase Complex Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Signal Transduction - physiology Sulfenic Acids - chemistry Sulfenic Acids - metabolism Sulfhydryl Compounds - chemistry Sulfhydryl Compounds - metabolism Sulfhydryl Reagents - metabolism
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