Identification And Characterization Of Methyl-H3K4Binding Protein

Histone methylation is known to function as docking sites for specific chromatin-associated proteins. The effector proteins are therefore responsible for interpreting the methylation code and thus mediate the biological effect of histone methylation. One of the best characterized histone methylation is H3K4methylation. The goal of my project is to identify and characterize the effector proteins that recruited (or repelled) by H3K4.Project1:A novel class of H3K4Me2binding proteins has been identified through the histone tail peptide pull-down assay, and then we demonstrated the protein sequences rich in acidic amino acid as a novel H3K4me2binding module. In addition, the H3K4me2binding activity is required for these proteins to associate with their target genes, and therefore involvement in transcriptional regulation.Project2:NuRD complex was identified as the major factor bound to unmethylated H3K4tail, implying a role of H3binding in targeting NuRD for its downstream transcriptional functions. But how NuRD interacts with H3is yet to be elucidated. Our data indicates that the MTA1/2/3subunits bridge the NuRD complex with histone H3through their C-terminal domain.