Graduate School of Medical Life Science, Yokohama City University

We are analyzing the structure of proteins and DNA related to transcription and chromatin structure by using NMR. Cytogenesis and cell differentiation are regulated at the transcriptional level, but in eukaryotes, changes of chromatin structure are important for transcriptional regulation. Telomere structure at the end of chromatin is also important for canceration and aging. We are elucidating these regulatory mechanisms at the atomic level based on the network between proteins on DNAs.

In recent years, it has become possible to analyze protein structures by NMR, and it has been clear that the crystal structure does not always reflect the solution structure in eukaryotic nuclear proteins. Especially in an aqueous solution, it has been known that the structure is formed by encountering a partner at random by itself. We called the structure (that called intrinsically disordered protein, intrinsically disordered protein, intrinsically unstructured protein or natively unfolded protein) intrinsically disordered protein here. Intrinsically disordered proteins have attracted attention in research on transcriptional activators.

In our laboratory, we will elucidate the dynamic structure and function control mechanism of intrinsically disordered proteins. We are targeting especially nuclear proteins in eukaryote, chromatin-related factors that alone have intrinsically disordered sites and fold as a whole with complex formation, nucleosomes, transcriptional activators, transcriptional repressors, and basic transcriptional factor. We will analyze the dynamic structure of the subject, the dynamic structure of the encounter complex, the dynamic structure of the intermediate and the dynamic structure of the specific complex, and the recognition mechanism of intrinsically disordered proteins using NMR.