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| Dataset | Description | Keywords | Number of Conditions | Reference |
|---|---|---|---|---|
| A balancing act: Interactions within NuA4/TIP60 regulate picNuA4 function in Saccharomyces cerevisiae and humans | The NuA4 lysine acetyltransferase complex acetylates histone and non-histone proteins and functions in transcription regulation, cell cycle progression, and DNA repair. NuA4 harbors an interesting duality in that its catalytic module can function independently and distinctly as picNuA4. At the molecular level, picNuA4 anchors to its bigger brother via physical interactions between the C-terminus of Epl1 and the HSA domain of Eaf1, the NuA4 central scaffolding subunit. This is reflected at the regulatory level, as picNuA4 can be liberated genetically from NuA4 by disrupting the Epl1-Eaf1 interaction. As such, removal of either Eaf1 or the Epl1 C-terminus offers a unique opportunity to elucidate the contributions of Eaf1 and Epl1 to NuA4 biology and in turn their roles in balancing picNuA4 and NuA4 activities. Using high-throughput genetic and gene expression profiling, and targeted functional assays to compare eaf1∆ and epl1-C∆ mutants, we found that EAF1 and EPL1 had both overlapping and distinct roles. Strikingly, loss of EAF1 or its HSA domain led to a significant decrease in the amount of picNuA4, while loss of the Epl1 C-terminus increased picNuA4 levels, suggesting starkly opposing effects on picNuA4 regulation. The eaf1∆ epl1-C∆ double mutants resembled the epl1-C∆ single mutants, indicating that Eaf1’s role in picNuA4 regulation depended on the Epl1 C-terminus. Key aspects of this regulation were evolutionary conserved, as truncating an Epl1 homolog in human cells increased the levels of other picNuA4 subunits. Our findings suggested a model in which distinct aspects of the Epl1-Eaf1 interaction regulated picNuA4 amount and activity. | histone modification | 10 | Lu PYT, et al. (2022) PMID:36066422 |
| A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation | Histone acetylation and deacetylation are among the principal mechanisms by which chromatin is regulated during transcription, DNA silencing, and DNA repair | genetic interaction, histone modification | 44 | Lin YY, et al. (2008) PMID:18676811 |
| A genome-wide housekeeping role for TFIID and a highly stress-related role for SAGA in Saccharomyces cerevisiae | TFIID and SAGA are the only two known yeast complexes that modify chromatin and deliver TBP to promoters | chromatin organization, histone modification | 1 | Huisinga KL and Pugh BF (2004) PMID:14992726 |
| A high-resolution view of transcription and chromatin states across distinct metabolic states in budding yeast | Under continuous, glucose-limited conditions, budding yeast exhibit robust metabolic cycles associated with major oscillations of gene expression and metabolic state | histone modification, transcription, chromatin organization | 202 | Kuang Z, et al. (2014) PMID:25173176 |
| A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme | The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function | histone modification | 3 | Watanabe S, et al. (2013) PMID:23580526 |
| A Key Role for Chd1 in Histone H3 Dynamics at the 3' Ends of Long Genes in Yeast | This SuperSeries is composed of the SubSeries listed below. | histone modification | 20 | Radman-Livaja M, et al. (2012) PMID:22807688 |
| A Key Role for Chd1 in Histone H3 Dynamics at the 3' Ends of Long Genes in Yeast (Flag-tagged histone H3 to total histone H3) | Chd proteins are ATP-dependent chromatin remodeling enzymes implicated in biological functions from transcriptional elongation to control of pluripotency | histone modification | 6 | Radman-Livaja M, et al. (2012) PMID:22807688 |
| A Key Role for Chd1 in Histone H3 Dynamics at the 3' Ends of Long Genes in Yeast (gene expression) | Chd proteins are ATP-dependent chromatin remodeling enzymes implicated in biological functions from transcriptional elongation to control of pluripotency | histone modification, chromatin organization | 2 | Radman-Livaja M, et al. (2012) PMID:22807688 |
| A Key Role for Chd1 in Histone H3 Dynamics at the 3' Ends of Long Genes in Yeast (H3K4me3 or H3K36me3 to input) | Chd proteins are ATP-dependent chromatin remodeling enzymes implicated in biological functions from transcriptional elongation to control of pluripotency | histone modification | 8 | Radman-Livaja M, et al. (2012) PMID:22807688 |
| A Key Role for Chd1 in Histone H3 Dynamics at the 3' Ends of Long Genes in Yeast (Rpb3 to input) | Chd proteins are ATP-dependent chromatin remodeling enzymes implicated in biological functions from transcriptional elongation to control of pluripotency | histone modification | 4 | Radman-Livaja M, et al. (2012) PMID:22807688 |