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Biochemical characterization of the protein-protein interaction between UTX and 53BP1
Jordan, Sam
Jordan, Sam
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Text, Honors papers, Chemistry, Department of
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Abstract
Embryonic stem cells are unique self-renewing cells that are able to differentiate into all
of the mature cells of the body. Our lab is interested in understanding the mechanisms
that regulate ES cell self-renewal and differentiation. One of the key mechanisms in this
process involves epigenetic factors, which mediate heritable changes in gene
expression without modifying the genomic sequence. UTX is an epigenetic factor
involved in the activation of genes that aid in stem cell differentiation. Additionally,
mutations at the UTX gene locus have been linked to various human cancers and the
developmental disorder the Kabuki syndrome. Preliminary data from our lab identified
53BP1 as a novel binding protein of UTX. 53BP1 is a key protein involved in the cellular
response to DNA double-stranded breaks. The results presented here show that UTX
localizes to 53BP1-positive DNA damage foci in different human cell lines, suggesting a
potential role for UTX in the DNA damage response. Surprisingly, UTX protein does not
localize to DNA damage foci in mice, suggesting the UTX-53BP1 binding is not
conserved in mouse models. Finally, this study successfully identifies the binding
domain of 53BP1 and attempts to identify the binding domain of UTX, thereby providing
insight into the molecular nature of this physical interaction.