Post-translational modifications (PTMs) of histones provide a controlled mechanism for regulating chromatin structure and dynamics. PTMs can rework direct interactions between DNA and histones and serve as docking sites for epigenomic readers and effectors. Binding of the readers to histone modifications can result in recruitment of multi-protein co-regulator complexes like the Nucleosome Remodeling and Deacetylase (NuRD) complex to specific genomic sites to mediate fundamental DNA-templated processes. Currently, however, our understanding of how the NuRD complex chooses its genomic target sites is limited.
In this project we aim to explore the interactions made by the NuRD with coregulatory proteins that themselves are capable of interacting with chromatin. We are using biochemical interaction assays and structural approaches to understand the mechanisms by which such proteins interact with the NuRD complex. Our data will help us build a mechanistic picture of how the NuRD complex selects its genomic targets and may offer opportunities to regulate NuRD function.