Binding and functional characteristics of two E-box motifs within the S100A6 (calcyclin) gene promoter.

Wiesława Leśniak, Jacek Kuźnicki

Journal: Journal of cellular biochemistry 2006;97(5):1017-24

PMID: 16288473

Abstract

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.

Address: Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, 3 Pasteur street, 02-093 Warsaw, Poland. [email protected]

DOI: 10.1002/jcb.20699

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MeSH Terms: Binding Sites, Cell Cycle Proteins, Cell Line, DNA-Binding Proteins, E-Box Elements, Gene Expression Regulation, Humans, Mutation, Palmitates, Phosphorylation, Promoter Regions, Genetic, Protein Binding, S100 Calcium Binding Protein A6, S100 Proteins, Transcription, Genetic, Upstream Stimulatory Factors