| First Author | Sayeed SK | Year | 2015 |
| Journal | Biochim Biophys Acta | Volume | 1849 |
| Issue | 6 | Pages | 583-9 |
| PubMed ID | 25779641 | Mgi Jnum | J:250881 |
| Mgi Id | MGI:6100267 | Doi | 10.1016/j.bbagrm.2015.03.002 |
| Citation | Sayeed SK, et al. (2015) C/EBPbeta (CEBPB) protein binding to the C/EBP|CRE DNA 8-mer TTGC|GTCA is inhibited by 5hmC and enhanced by 5mC, 5fC, and 5caC in the CG dinucleotide. Biochim Biophys Acta 1849(6):583-9 |
| abstractText | During mammalian development, some methylated cytosines (5mC) in CG dinucleotides are iteratively oxidized by TET dioxygenases to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC), and 5-carboxylcytosine (5caC). The effect of these cytosine oxidative products on the sequence-specific DNA binding of transcription factors is being actively investigated. Here, we used the electrophoretic mobility shift assay (EMSA) to examine C/EBPalpha and C/EBPbeta homodimers binding to all 25 chemical forms of a CG dinucleotide for two DNA sequences: the canonical C/EBP 8-mer TTGCGCAA and the chimeric C/EBPCRE 8-mer TTGCGTCA. 5hmC in the CG dinucleotide in the C/EBPCRE motif 8-mer TGACGCAA inhibits binding of C/EBPbeta but not C/EBPalpha. Binding was increased by 5mC, 5fC and 5caC. Circular dichroism monitored thermal denaturations for C/EBPbeta bound to the C/EBPCRE motif confirmed the EMSA. The structural differences between C/EBPalpha and C/EBPbeta that may account for the difference in binding 5hmC in the 8-mer TGACGCAA are explored. |
