| Literature DB >> 25779641 |
Syed Khund Sayeed1, Jianfei Zhao1, Bangalore K Sathyanarayana2, Jaya Prakash Golla1, Charles Vinson3.
Abstract
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/EBPα and C/EBPβ homodimers binding to all 25 chemical forms of a CG dinucleotide for two DNA sequences: the canonical C/EBP 8-mer TTGC|GCAA and the chimeric C/EBP|CRE 8-mer TTGC|GTCA. 5hmC in the CG dinucleotide in the C/EBP|CRE motif 8-mer TGAC|GCAA inhibits binding of C/EBPβ but not C/EBPα. Binding was increased by 5mC, 5fC and 5caC. Circular dichroism monitored thermal denaturations for C/EBPβ bound to the C/EBP|CRE motif confirmed the EMSA. The structural differences between C/EBPα and C/EBPβ that may account for the difference in binding 5hmC in the 8-mer TGAC|GCAA are explored. Published by Elsevier B.V.Entities:
Keywords: 5hmC, 5fC, 5caC, carboxylation; 5mC; Basic-leucine zipper; C/EBP|CRE motif; C/EBPβ homodimer; CG dinucleotide; DNA binding
Mesh：
Substances：
Year: 2015 PMID： 25779641 PMCID： PMC7857639 DOI： 10.1016/j.bbagrm.2015.03.002
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002