{Reference Type}: Journal Article
{Title}: Carboxylation of cytosine (5caC) in the CG dinucleotide in the E-box motif (CGCAG|GTG) increases binding of the Tcf3|Ascl1 helix-loop-helix heterodimer 10-fold.
{Author}: Golla JP;Zhao J;Mann IK;Sayeed SK;Mandal A;Rose RB;Vinson C;
{Journal}: Biochem Biophys Res Commun
{Volume}: 449
{Issue}: 2
{Year}: Jun 2014 27
{Factor}: 3.322
{DOI}: 10.1016/j.bbrc.2014.05.018
{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 ~10-fold. These results highlight a potential function of the oxidative products of 5mC, changing the DNA binding of sequence-specific transcription factors.