Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10754792 | Biochemical and Biophysical Research Communications | 2014 | 8 Pages |
Abstract
Three oxidative products of 5-methylcytosine (5mC) occur in mammalian genomes. We evaluated if these cytosine modifications in a CG dinucleotide altered DNA binding of four B-HLH homodimers and three heterodimers to the E-Box motif CGCAG|GTG. We examined 25 DNA probes containing all combinations of cytosine in a CG dinucleotide and none changed binding except for carboxylation of cytosine (5caC) in the strand CGCAG|GTG. 5caC enhanced binding of all examined B-HLH homodimers and heterodimers, particularly the Tcf3|Ascl1 heterodimer which increased binding â¼10-fold. These results highlight a potential function of the oxidative products of 5mC, changing the DNA binding of sequence-specific transcription factors.
Keywords
dsDNAEMSA5fCAchaete-scute homolog 1TCF3Ascl15hmCTcf4ssDNA5caC5mC5-formylcytosine5-Methylcytosine5-hydroxymethylcytosine5-carboxylcytosineSingle-stranded DNAdouble-stranded DNAElectrophoretic mobility shift assayDNA bindingBasic-helix-loop-helixE-boxcytosineTranscription factor 4transcription factor 3Carboxylation
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Authors
Jaya Prakash Golla, Jianfei Zhao, Ishminder K. Mann, Syed K. Sayeed, Ajeet Mandal, Robert B. Rose, Charles Vinson,