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The nuclear phosphoprotein DEK is abundantly present in cells and is implicated in diseases including leukemia and autoimmune disorders. DEK has three highly acidic amino acid domains and inhibits histone acetyltransferase activity by binding directly to histones. In a previous study, differentially regulated proteins under DEK knockdown conditions, including the up-regulated protein 1-cys peroxiredoxin (1-cys Prx), were identified by proteome analysis. Here, an in vivo reporter assay with short hairpin RNA-mediated DEK knockdown revealed that DEK negatively regulated 1-cys Prx transcription, and that the NF-κB subunit p65 had a synergistic effect on this DEK-mediated repression. Both proteins are recruited to the 1-cys Prx promoter region and regulate its transcription. Our study demonstrates that DEK modulates the transcriptional regulation of the target gene through protein interaction with other regulatory proteins.

Transcriptional regulation of 1-cys peroxiredoxin by the proto-oncogene protein DEK