Title : Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.

Pub. Date : 2007 Jul 3

PMID : 17555331






5 Functional Relationships(s)
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1 Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress. Cysteine tumor protein p53 Homo sapiens
2 Mass spectrometry of GSH-modified p53 protein identified cysteines 124, 141, and 182, all present in the proximal DNA-binding domain, as the sites of glutathionylation. Cysteine tumor protein p53 Homo sapiens
3 Biotinylated maleimide also reacted rapidly with Cys141, implying that this is the most reactive cysteine on the p53 surface. Cysteine tumor protein p53 Homo sapiens
4 The glutathionylatable cysteines were found to exist in a negatively charged microenvironment in cellular p53. Cysteine tumor protein p53 Homo sapiens
5 These results show for the first time that shielding of reactive cysteines contributes to a negative regulation for human p53 and imply that such an inactivation of the transcription factor may represent an acute defensive response with significant consequences for oncogenesis. Cysteine tumor protein p53 Homo sapiens