@article{3810,
  keywords = {Humans, Binding Sites, Transcription Factors, DNA-Binding Proteins, Adenosine Triphosphatases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Chromosomal Proteins, Non-Histone, Cysteine, Amino Acid Motifs, Histones, Nucleosomes, Chromatin Assembly and Disassembly},
  author = {Hai Dao and Barbara Dul and Geoffrey Dann and Glen Liszczak and Tom Muir},
  title = {A basic motif anchoring ISWI to nucleosome acidic patch regulates nucleosome spacing.},
  abstract = { <p>Recent studies have implicated the nucleosome acidic patch in the activity of ATP-dependent chromatin remodeling machines. We used a photocrosslinking-based nucleosome profiling technology (photoscanning) to identify a conserved basic motif within the catalytic subunit of ISWI remodelers, SNF2h, which engages this nucleosomal epitope. This region of SNF2h is essential for chromatin remodeling activity in a reconstituted biochemical system and in cells. Our studies suggest that the basic motif in SNF2h plays a critical role in anchoring the remodeler to the nucleosomal surface. We also examine the functional consequences of several cancer-associated histone mutations that map to the nucleosome acidic patch. Kinetic studies using physiologically relevant heterotypic nucleosomal substrates ({\textquoteright}Janus{\textquoteright} nucleosomes) indicate that these cancer-associated mutations can disrupt regularly spaced chromatin structure by inducing ISWI-mediated unidirectional nucleosome sliding. These results indicate a potential mechanistic link between oncogenic histones and alterations to the chromatin landscape.</p> },
  year = {2020},
  journal = {Nat Chem Biol},
  volume = {16},
  pages = {134-142},
  month = {2020 Feb},
  issn = {1552-4469},
  doi = {10.1038/s41589-019-0413-4},
  language = {eng},
}