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Affinity Characterization of TTD Domain of UHRF2 Histone Reader Protein.
Author(s) -
Petzold Timothy Samuel
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.755.13
Subject(s) - linker , histone , epigenetics , oncogene , chemistry , dissociation constant , histone h3 , phd finger , microbiology and biotechnology , suppressor , biology , biochemistry , computational biology , gene , receptor , transcription factor , zinc finger , computer science , cell cycle , operating system
One proposed method for anticancer drug development is to target epigenetic proteins, which regulate genome expression and are involved in various cancers. The ubiquitous reader protein UHRF1 (Ubiquitin Like With PHD And Ring Finger Domains) is identified as an oncogene and its binding affinity to histone H3 has been well‐determined via its PHD and TTD domains. The homologue, UHRF2, is noted to have properties of a tumor‐suppressor and oncogene, dependent on the cancer, but its affinity for H3 has not been assessed. In this study, we characterized the binding affinity of the TTD domain of UHRF2. The dissociation constant between H3K9me3 and TTD of UHRF2 was determined by fluorescence polarization assays. Interestingly, our study suggests that the linker portion between TTD and PHD inhibits binding of the TTD to H3. This linker region may provide a promising approach for regulating the activity of UHRF2.