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
| Autor: | Jianfei Zhao, Ajeet Mandal, Ishminder Mann, Charles Vinson, Jaya Prakash Golla, Syed Khund Sayeed, Robert B. Rose |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Molecular Sequence Data Biophysics E-box Oxidative phosphorylation Biology Biochemistry Article E-Box Elements Cytosine chemistry.chemical_compound Basic Helix-Loop-Helix Transcription Factors Animals Humans Amino Acid Sequence Molecular Biology Transcription factor Base Sequence Basic helix-loop-helix Circular Dichroism Hybridization probe Cell Biology chemistry Carboxylation 5-Methylcytosine Protein Multimerization Dinucleoside Phosphates DNA Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 449:248-255 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2014.05.018 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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