H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement
- Janelia Research Campus, Howard Hughes Medical Institute, United States
- National Institutes of Health, United States
Abstract
The histone variant H2A.Z is a universal mark of gene promoters, enhancers and regulatory elements in eukaryotic chromatin. The chromatin remodeler SWR1 mediates site-specific incorporation of H2A.Z by a multi-step histone replacement reaction, evicting histone H2A-H2B from the canonical nucleosome and depositing the H2A.Z-H2B dimer. Binding of both substrates-the canonical nucleosome and the H2A.Z-H2B dimer, is essential for activation of SWR1. We found that SWR1 primarily recognizes key residues within the α2 helix in the histone-fold of nucleosomal histone H2A, a region not previously known to influence remodeler activity. Moreover, SWR1 interacts preferentially with nucleosomal DNA at superhelix location 2 on the nucleosome face distal to its linker-binding site. Our findings provide new molecular insights on recognition of the canonical nucleosome by a chromatin remodeler, and have implications for ATP-driven mechanisms of histone eviction and deposition.
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H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement
eLife 4:e06845.
https://doi.org/10.7554/eLife.06845
