Jean-Baptiste, Uriel2017-08-142017-08-142017https://hdl.handle.net/1794/225851 page posterEukaryotic DNA is packaged into chromatin to fit in the nucleus. One of the organizational subunits of chromatin are nucleosomes, which are composed of DNA wrapped around histone proteins. These nucleosomes can be rearranged by proteins called chromatin remodelers. For this project, we looked at the nucleosome remodeling protein Chd1. It has been shown that the Chd1 protein fused with a foreign DNA binding domain (DBD) can remodel nucleosomes toward the specific site of that foreign DBD (McKnight et al. 2011). We are using this knowledge to design fusion proteins where the DBD of Chd1 has been replaced with a variety of different domains, targeting Chd1 to different sites in the genome. The specific fusion for this project used the DBD of Hsf1, a protein that recognizes a conserved heat shock element (HSE) motif in the yeast S. cerevisiae. When induced, Hsf1 turns on stress genes that allow the cells to survive in stressful environments. With this foreign DBD fused to the Chd1 remodeler, we aim to target nucleosomes to genomic HSE sites, blocking access for Hsf1 and thereby modulating the heat shock response. This project will demonstrate the feasibility of using engineered nucleosome positioning to control a physiological response in vivo.enCreative Commons BY-NC-ND 4.0-USChd1Chromatin RemodelerHsflOther