Wilms tumor protein recognizes 5-carboxylcytosine within a specific DNA sequence
By H. Hashimoto, Y. Olanrewaju, Yu Zheng, G. Wilson, Xing Zhang, Xiaodong Cheng. 2014
129 citations recorded by the source corpus.
Hashimoto et al. investigated the response of the zinc finger DNA-binding domains of transcription factors early growth response protein 1 (Egr1) and Wilms tumor protein 1 (WT1) to different forms of modified cytosine within their recognition sequence. 5-Carboxylcytosine (5caC) affected the two proteins differently, abolishing binding by Egr1 but not by WT1. In Egr1, a negatively charged glutamate conflicts with the negatively charged carboxylate of 5caC, whereas the corresponding glutamine of WT1 interacts with this group favorably.
Subfields: Molecular Biology
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Citations in the corpus
- Impact of cytosine methylation on DNA binding specificities of human transcription factors (2017, neutral): “These results are consistent with the earlier finding that TF binding induces loss of local DNAmethylation, potentially using the TET/TDGdependent demethylation pathway (7, 49, 50).”
- Role of TET enzymes in DNA methylation, development, and cancer (2016, background): “In addition, oxidation of cytosines in the DNA-binding motif of the TF Wilms tumor 1 (WT1; to 5hmC and 5fC but not 5caC) effectively disrupts protein–DNA interaction (Hashimoto et al. 2014a).”