The paper, , was designated as a “Breakthrough Article” by NAR in 2020 which is an honor given to the top 1-2% of all papers.
Thenucleosomeis the fundamental packaging unit of our genome. Proteins that control gene expression and repair of DNA damage must bind tonucleosomesto perform their functions. While studies of individual proteins bound to thenucleosomehave shown that an acidic patch made of negatively charged atoms on thenucleosomemay be a common site for protein binding, the pervasiveness of this acidic patch binding and whetherothernucleosomebindinghot-spotsexist remained unclear. This study describes an elegant proteomics screen that establishes the universal principles ofnucleosomerecognition.The authors prepared a library of nucleosomes,each containing a cluster of mutations within a different patch on thenucleosomedisk surface. Quantitative mass spectrometry was then used to compare the abundance of proteins that interact with each of thenucleosomesin the library. By analyzing how each cluster of mutations influencednucleosomebinding proteome-wide,the authors paired hundredsofnucleosomebinding proteins with the specificnucleosomesurface requirements.Thenucleosomeacidic patch,was critical forthe majority ofnucleosomebinding proteins, often in concert with two adjacent, newly identified hot-spots. This comprehensivenucleosomeinteractomescreen uncovers the general rules governing recognition of the fundamental unit of the genome.


AleksandraSkrajnaPhDis an American Cancer Society postdoctoral fellow in the .
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