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| Status |
Public on Apr 15, 2013 |
| Title |
A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme |
| Organism |
Saccharomyces cerevisiae W303 |
| Experiment type |
Genome binding/occupancy profiling by high throughput sequencing
|
| Summary |
The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange where either H2A.Z or H2A can be exchanged from nucleosomes. This result is confirmed in vivo, where genome-wide analysis demonstrates widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a “lock” that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators.
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| Overall design |
H2A.Z ChIP seq experiments in mutants with constitutive H3K56ac
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| Contributor(s) |
Watanabe S, Radman-Livaja M, Rando O, Petersen C |
| Citation(s) |
23580526 |
| |
| Submission date |
Jan 31, 2013 |
| Last update date |
May 15, 2019 |
| Contact name |
Marta Radman-Livaja |
| E-mail(s) |
mrl5374@gmail.com
|
| Phone |
+33434359667
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| Organization name |
CNRS
|
| Department |
IGMM
|
| Street address |
1919 route de Mende
|
| City |
Montpellier |
| ZIP/Postal code |
34293 |
| Country |
France |
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| Platforms (1) |
| GPL16574 |
Illumina Genome Analyzer (Saccharomyces cerevisiae W303) |
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| Samples (3) |
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| Relations |
| BioProject |
PRJNA188180 |
| SRA |
SRP018330 |
