E-GEOD-49183 - Nucleosome free DNA- and acetyl histone-binding components recruit SWR1 to yeast promoters for H2A.Z replacement

Released on 16 September 2013, last updated on 3 June 2014
Saccharomyces cerevisiae
Samples (16)
Array (1)
Protocols (6)
The histone variant H2A.Z is a genome-wide signature of nucleosomes proximal to eukaryotic regulatory DNA. While the multi-subunit SWR1 chromatin remodeling complex is known to catalyze ATP-dependent deposition of H2A.Z, the mechanism of recruitment to S. cerevisiae promoters has been unclear. A sensitive assay for competitive binding of di-nucleosome substrates revealed that SWR1 preferentially binds long nucleosome-free DNA adjoining core particles, allowing discrimination of gene promoters over gene bodies. We traced the critical DNA binding component of SWR1 to the conserved Swc2/YL1 subunit, whose activity is required for both SWR1 binding and H2A.Z incorporation in vivo. Histone acetylation by NuA4 enhances SWR1 binding, but the interaction with nucleosome-free DNA is the major determinant. ‘Hierarchical cooperation’ between high affinity DNA- and low affinity histone modification-binding factors may reconcile the large disparity in affinities for chromatin substrates, and unify classical control by DNA-binding factors with post-translational histone modifications and ATP-dependent nucleosome mobility. Swr1 TAP IF of various mutants
Experiment type
ChIP-chip by tiling array 
Anand Ranjan <ranjana@mail.nih.gov>, A Ranjan, C Wu, G Mizuguchi, P Fitzgerald
Investigation descriptionE-GEOD-49183.idf.txt
Sample and data relationshipE-GEOD-49183.sdrf.txt
Raw data (1)E-GEOD-49183.raw.1.zip
Processed data (1)E-GEOD-49183.processed.1.zip
Array designA-GEOD-17487.adf.txt