Aleksandra Skrajna, Dennis Goldfarb, Katarzyna M Kedziora, Emily M Cousins, Gavin D Grant, Cathy J Spangler, Emily H Barbour, Xiaokang Yan, Nathaniel A Hathaway, Nicholas G Brown, Jeanette G Cook, Michael B Major, and Robert K McGinty
Nucleic Acids Research, gkaa544, doi: 10.1093/nar/gkaa544
A growing number of structural analyses and related studies have shed light on how proteins interact with the fundamental unit of chromatin, the nucleosome. While such work has suggested that an acidic patch on the nucleosome disk surface may be a hot-spot for nucleosome binding, it has remained unclear how many proteins bind to this nucleosome surface and whether other hot-spots exist and remain undiscovered. The authors of the current study describe a comprehensive nucleosome interactome screen to define the universal principles of nucleosome interactions. Rather than a typical characterization of one interaction at a time, they used nucleosome affinity proteomics with a library of mutant nucleosomes that collectively disrupts all exposed histone surfaces to 1) define the hot-spots for nucleosome binding proteome-wide, and 2) establish a comprehensive set of proteins that bind the nucleosome and the nucleosome surfaces required for each interaction.