Human p53 Is Inhibited by Glutathionylation of Cysteines Present in the Proximal DNA-Binding Domain during Oxidative Stress

The cellular mechanisms that modulate the redox state of p53 tumor suppressor remain unclear, although its DNA binding function is known to be strongly inhibited by oxidative and nitrosative stresses. We show that human p53 is subjected to a new and reversible posttranslational modification, namely,...

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Veröffentlicht in:	Biochemistry (Easton) 2007-07, Vol.46 (26), p.7765-7780
Hauptverfasser:	Velu, Chinavenmeni S, Niture, Suryakant K, Doneanu, Catalin E, Pattabiraman, Nagarajan, Srivenugopal, Kalkunte S
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylcysteine - pharmacology Amino Acid Sequence Binding Sites Buthionine Sulfoximine - pharmacology Camptothecin - pharmacology Cell Line, Tumor Cross-Linking Reagents - chemistry Cysteine - chemistry Diamide - pharmacology DNA Damage - drug effects DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism Glutaral - chemistry Glutathione - analogs & derivatives Glutathione - chemistry Glutathione - pharmacology Glutathione Disulfide - chemistry Humans Hydrogen Peroxide - pharmacology Models, Molecular Oxidative Stress - drug effects Oxidative Stress - physiology Phosphorylation Recombinant Proteins - metabolism Tandem Mass Spectrometry tert-Butylhydroperoxide - pharmacology Tumor Suppressor Protein p53 - antagonists & inhibitors
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