The CpG Dinucleotide Adjacent to a κB Site Affects NF-κB Function through Its Methylation
AbstractNF-κB is an important transcription factor that plays critical roles in cell survival, proliferation, inflammation, and cancers. Although the majority of experimentally identified functional NF-κB binding sites (κB sites) match the consensus sequence, there are plenty of non-functional NF-κB consensus sequences in the genome. We analyzed the surrounding sequences of the known κB sites that perfectly match the GGGRNNYYCC consensus sequence and identified the nucleotide at the -1 position of κB sites as a key contributor to the binding of the κB sites by NF-κB. We demonstrated that a cytosine at the -1 position of a κB site (-1C) could be methylated, which thereafter impaired NF-κB binding and/or function. In addition, all -1C κB sites are located in CpG islands and are conserved during evolution only when they are within CpG islands. Interestingly, when there are multiple NF-κB binding possibilities, methylation of -1C might increase NF-κB binding. Our finding suggests that a single nucleotide at the -1 position of a κB site could be a critical factor in NF-κB functioning and could be exploited as an additional manner to regulate the expression of NF-κB target genes. View Full-Text
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Wang, T.; Li, J.; Ding, K.; Zhang, L.; Che, Q.; Sun, X.; Dai, Y.; Sun, W.; Bao, M.; Wang, X.; Yang, L.; Li, Z. The CpG Dinucleotide Adjacent to a κB Site Affects NF-κB Function through Its Methylation. Int. J. Mol. Sci. 2017, 18, 528.
Wang T, Li J, Ding K, Zhang L, Che Q, Sun X, Dai Y, Sun W, Bao M, Wang X, Yang L, Li Z. The CpG Dinucleotide Adjacent to a κB Site Affects NF-κB Function through Its Methylation. International Journal of Molecular Sciences. 2017; 18(3):528.Chicago/Turabian Style
Wang, Tao; Li, Jinge; Ding, Ke; Zhang, Li; Che, Qiuru; Sun, Xiuming; Dai, Yumeng; Sun, Wei; Bao, Meiying; Wang, Xiaochun; Yang, Liquan; Li, Zhiwei. 2017. "The CpG Dinucleotide Adjacent to a κB Site Affects NF-κB Function through Its Methylation." Int. J. Mol. Sci. 18, no. 3: 528.
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