Yi’s interests are focused on determining the molecular and structural mechanisms by which chromatin-associating proteins recognize post-transcriptional modifications (PTMs). She is also interested in characterizing the biological outcomes and pathological consequences of PTM-reader domain interactions. Most recently, Yi was involved in several collaborative studies, which elucidated the functions of the ZZ domain as a histone reader and a sensor of protein degradation signals. For instance, Yi and colleagues revealed that the ZZ domain binds to the N-terminal histone H3 tail and modulates the substrate specificity of the adjacent HAT domain in histone acetyltransferase p300. This work provides key insights into understanding the mechanism of action of p300, particularly the selective acetylation of H3K27 at enhancer regions.
Yi has a strong background in structural biology, biophysics, biochemistry, and molecular biology. She is also trained in chromatin and cellular biology and has experience in studying nucleosome remodelers, membrane proteins and adaptor proteins. Her topics of expertise include epigenetics, chromatin structure, gene expression, and protein degradation.