Master of Science
Dr. Shawn Li
It has been 50 years since the first histone methylation was identified. From then, numerous studies have verified that histone methylation neutralizes the positive charges of lysine, alters chromatin architectures, and recruits other DNA binding complexes. In this study, we examined the molecular basis of a histone demethylase – KDM5B in both its substrate and binding machineries. We hypothesized that KDM5B has alternative binding partners and substrates besides its known target H3K4me3. By utilizing biochemical approaches such as in vitro pull-down assays and fluorescence polarization assays, we were able to identify potential KDM5B binding partners – H2BK43me0/2. Also, we reinvestigated the recognition mechanisms and found that the unmodified H2BK43me0 was a potential binding site of PHD1 and PHD2 while H2BK43me2 was a potential partner of PHD1. In addition, we observed H2BK43me2 demethylation via KDM5B in MCF7 cells. Together, our preliminary results suggested that H2BK43me2 was an alternative binding partner and substrate of KDM5B.
Fang, Qi, "Identification of novel binding partners and substrates of histone H3K4 specific demethylase KDM5B/JARID1B" (2017). Electronic Thesis and Dissertation Repository. 5061.