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Molecular Characterization of UHRF1 and UHRF2
Author(s) -
Winkler Alyssa,
Albaugh Brittany
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.755.11
Subject(s) - histone , epigenetics , phd finger , affinities , lysine , mutagenesis , biology , biochemistry , gene , amino acid , genetics , computational biology , chemistry , zinc finger , mutation , transcription factor
UHRF1 and UHRF2 are multidomain epigenetic proteins that function to bind modified histones and subsequently regulate gene expression, particular those involved in cancer development. The Tandem‐Tudor Domain (TTD) and Plant Homeo Domain (PHD), are structural motifs that are proposed to bind trimethylated lysine‐9 and unmodified lysine 4 on histone H3, respectively. Here, we investigate the functional and structural interactions between the PHD and TTD UHRF1/2 protein domains and modified histones. Using fluorescence polarization assays, we have assessed the relative binding affinities for the linked TTD‐PHD domains of both UHRF1 and UHRF2, and found that there was no significant difference in binding affinities between the UHRF1 and UHRF2 TTD‐PHD linked domains. We continued investigating specific structural roles within the domains through mutagenesis of amino acids of interest.