The protein p53 is an important redox-active transcription factor that is known to differentially dissociate from its consensus sequence upon DNA-mediated oxidation.  The lower the oxidation potential of the consensus sequence purine region, the greater DNA-mediated oxidative dissociation of  p53 is observed. Greater p53 oxidative dissociation occurs in the order of decreasing oxidation potential, as studied through EMSA and guanine oxidation PAGE  in unnatural and natural p53 consensus sequence oligonucleotides in vitro.  To determine whether p53 dissociation observed in vitro correlated to changes in mRNA production in vivo,  HCT116N cells under genomic oxidative stress were studied by RT-qPCR. Changes in gene regulation correlated to results observed in gel shift assays.  DNA charge transport can be sensed and quenched by DNA-bound proteins depending on the oxidation potential created by the DNA sequence to which they are bound, indicating that DNA sequence identity can be used as a means of regulation.

DNA-mediated oxidation of p53 is regulated by DNA sequence

243rd National Meeting (2012)

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