Extranucleosomal DNA Enhances The Activity Of The LSD1/CoREST Histone Demethylase Complex
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FUNCTIONAL RECOGNITION OF THE NUCLEOSOME BY CHROMATIN FACTOR
The LSD1/CoREST (lysine specific demethylase 1/Co-repressor element 1 silencing transcription factor) complex is a histone H3K4 mono- and di- demethylase that is associated with transcriptional repression. Previous work has shown that while LSD1 can demethylate peptide substrates, CoREST is required for LSD1 demethylase activity on the nucleosome.
STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF LSD1/COREST
In this dissertation, I provide insights into how the LSD1/CoREST complex interacts with the nucleosome via biochemical and structural approaches. My studies of LSD1/CoREST s enzymatic activity and nucleosome binding show that extranucleosomal DNA dramatically enhances the activity of LSD1/CoREST and that LSD1/CoREST requires DNA beyond the