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Evolution and divergence of the structural and physical properties of DNA binding by methyl-cytosine binding domain family members 2 and 3

Posted on:2015-07-11Degree:Ph.DType:Dissertation
University:Virginia Commonwealth UniversityCandidate:Cramer, Jason MatthewFull Text:PDF
GTID:1474390017491496Subject:Chemistry
Abstract/Summary:
The studies presented in this dissertation, Evolution And Divergence Of The Structural And Physical Properties Of DNA Binding By Methyl-Cytosine Binding Domain Family Members 2 And 3, pertain primarily to two key epigenetic regulators involved with the biological interpretation of methylated DNA marks. We provide insights into the emergence and evolution of the MBD2 and MBD3 and how those molecular entities influence heritable changes in gene activity. We further provide details regarding the mystery surrounding MBD3 function and the MBD2-mediated capacity of primitive animals to carry out methylation-specific epigenetic mechanisms. In chapter two, we describe the DNA binding properties of MBD2 and MBD3. This study provides information regarding previously unidentified MBD3 binding properties and potential biological function. In chapter three, we show that sponges demonstrate a MBD2-mediated capacity for binding methylated DNA sites, recruit NuRD components in vitro, and knockdown of MBD2 in the freshwater desmosponge, Ephydatia muelleri, promotes an abnormal growth phenotype.
Keywords/Search Tags:DNA binding, Evolution, MBD2, MBD3
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