@article{THESIS,
      recid = {1657},
      author = {Malecek, Kathryn Elizabeth},
      title = {Characterization of oxidized methylcytosine binding  protein activities in the mammalian brain and stem cells},
      publisher = {The University of Chicago},
      school = {Ph.D.},
      address = {2016-06},
      number = {THESIS},
      pages = {185},
      abstract = {5-Methylcytosine embedded in mammalian DNA represses local  transcription by recruiting modification-specific binding  partners. Its active removal is initiated by sequential  oxidation of the 5-methyl group by TET enzymes to produce  three oxidized species, collectively referred to as [ox]mC.  Although rare, the distribution of [ox]mC modifications is  tissue-, gene-, and coding strand-specific and distinct  from 5-methylcytosine, suggesting unique functions. To  examine this possibility, I fractionated mammalian brain  extracts to discover, isolate and characterize binding  partners specific for [ox]mC. This purification reveals  remarkably specific factors that are selective for each of  the three oxidation states and sensitive to the  5-modification state on each strand. I demonstrate that one  such factor, WDR76, is a highly  5-hydroxymethylcytosine-specific binding protein. I have  begun to lay the foundation for further mechanistic studies  of these specific binding proteins in mouse embryonic stem  cells and leukemia. My results provide an essential bridge  from studies of the distribution of [ox]mC and the effects  of TET knockouts, to the possible functions of [ox]mC  recognition in gene regulation or chromatin signaling.},
      url = {http://knowledge.uchicago.edu/record/1657},
      doi = {https://doi.org/10.6082/uchicago.1657},
}