Identification and characterization of histone globular domain-binding proteins

Abstract

Until now, interacting proteins of globular domain histone modification have been rarely identified because of its structural technical limitations. Recently, the amber codon suppression method has been developed to overcome the structural limitations and I will apply this method to my research. The site specifically modified nucleosome is reconstituted and pulled down with nuclear extracts. First I focused on the most famous and much studied H3K56Ac and H3K79Me. Before discovering the interaction candidate proteins, I found the effect of H3K56Ac and H3K79Me on transcription efficiency. Both histone modifications are characterized by the activation of transcription. Therefore, finding a protein that binds directly to these modifications will provide an in-depth understanding of transcription regulation mechanisms. In addition, various in vitro assays developed through this study will be the leading studies in the epigenetic study field.