@inbook{7f7c5518f17141eb947672e832eaf4f4,
title = "Characterization of How DNA Modifications Affect DNA Binding by C2H2 Zinc Finger Proteins",
abstract = "Much is known about vertebrate DNA methylation and oxidation; however, much less is known about how modified cytosine residues within particular sequences are recognized. Among the known methylated DNA-binding domains, the Cys2-His2 zinc finger (ZnF) protein superfamily is the largest with hundreds of members, each containing tandem ZnFs ranging from 3 to > 30 fingers. We have begun to biochemically and structurally characterize these ZnFs not only on their sequence specificity but also on their sensitivity to various DNA modifications. Rather than following published methods of refolding insoluble ZnF arrays, we have expressed and purified soluble forms of ZnFs, ranging in size from a tandem array of two to six ZnFs, from seven different proteins. We also describe a fluorescence polarization assay to measure ZnFs affinity with oligonucleotides containing various modifications and our approaches for cocrystallization of ZnFs with oligonucleotides.",
keywords = "C2H2 zinc finger, DNA methylation, DNA modification, Epigenetics, Ionic strength, Polyethylenimine",
author = "A. Patel and H. Hashimoto and X. Zhang and X. Cheng",
note = "Funding Information: We sincerely thank Yusuf Olatunde Olanrewaju and Yiwei Liu for their early efforts in purifying soluble ZnF proteins. This work was supported by grant from the National Institutes of Health GM049245-22 to X.C. (who is a Georgia Research Alliance Eminent Scholar). Publisher Copyright: {\textcopyright} 2016 Elsevier Inc.",
year = "2016",
doi = "10.1016/bs.mie.2016.01.019",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "387--401",
booktitle = "Methods in Enzymology",
}