An atomic model of a ubiquitinated and dimethylated histone core particle with bound 53BP1 built into a cryo-EM density map.
The laboratories of John Rubinstein and Frank Sicheri (Biochemistry), and Dan Durocher (Molecular Genetics) have used electron cryomicroscopy (cryo-EM) to determine the structure of the DNA-damage recognizing protein 53BP1 bound to modified nucleosome core particles. The work, published in Nature (http://www.nature.com/nature/journal/vaop/ncurrent/full/nature18951.html), was led by postdoctoral fellow Marcus Wilson and research associate Samir Benlekbir and provides the first structural insight into how dimethylation and ubiquitination of nucleosomes in response to DNA damage recruits 53BP1, initiating repair of the damage. The structure was determined by cryo-EM at 4.5 Å resolution, which approaches the resolutions that can be determined by X-ray crystallography.
