Binding and functional characteristics of two E-box motifs within the S100A6 (calcyclin) gene promoter.
S100A6 (calcyclin) is a small calcium-binding protein of the S100 family often associated with cancer and metastasis. We have previously shown that the E-box sequence at position -283/-278 of the S100A6 gene promoter interacts with USF transcription factor and contributes to promoter transcriptional activity. We now present evidence that a second E-box motif at position -593/-588 of the promoter also binds USF and that the USF1/USF2 heterodimer is the prevailing dimeric form of the transcription factor bound. Using the chromatin immunoprecipitation assay (ChIP), we show that USF is bound in vivo to the E-box regulatory element(s). Depletion of the endogenous USF pool by means of a decoy oligonucleotide evokes a severe inhibition of S100A6 gene promoter activity. Furthermore, we show that S100A6 gene promoter activity can be stimulated by palmitate and that mutation of the -283/-278 E-box sequence completely blocks this stimulation.[1]References
- Binding and functional characteristics of two E-box motifs within the S100A6 (calcyclin) gene promoter. Leśniak, W., Kuźnicki, J. J. Cell. Biochem. (2006) [Pubmed]
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