Yng1 PHD Finger Binding to H3 Trimethylated at K4 Promotes NuA3 HAT Activity at K14 of H3 and Transcription at a Subset of Targeted ORFs

Posttranslational histone modifications participate in modulating the structure and function of chromatin. Promoters of transcribed genes are enriched with K4 trimethylation and hyperacetylation on the N-terminal tail of histone H3. Recently, PHD finger proteins, like Yng1 in the NuA3 HAT complex, w...

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Published in:Molecular cell 2006-12, Vol.24 (5), p.785-796
Main Authors: Taverna, Sean D., Ilin, Serge, Rogers, Richard S., Tanny, Jason C., Lavender, Heather, Li, Haitao, Baker, Lindsey, Boyle, John, Blair, Lauren P., Chait, Brian T., Patel, Dinshaw J., Aitchison, John D., Tackett, Alan J., Allis, C. David
Format: Article
Language:English
Subjects:
Chromatin Immunoprecipitation
DNA
Genome, Fungal - genetics
Histone Acetyltransferases - genetics
Histone Acetyltransferases - metabolism
Histones - chemistry
Histones - metabolism
Methylation
Models, Molecular
Mutation
Nuclear Magnetic Resonance, Biomolecular
Open Reading Frames - genetics
Promoter Regions, Genetic - genetics
Protein Binding
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Sensitivity and Specificity
Transcription Factors - chemistry
Transcription Factors - genetics
Transcription Factors - metabolism
Transcription, Genetic
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Summary:Posttranslational histone modifications participate in modulating the structure and function of chromatin. Promoters of transcribed genes are enriched with K4 trimethylation and hyperacetylation on the N-terminal tail of histone H3. Recently, PHD finger proteins, like Yng1 in the NuA3 HAT complex, were shown to interact with H3K4me3, indicating a biochemical link between K4 methylation and hyperacetylation. By using a combination of mass spectrometry, biochemistry, and NMR, we detail the Yng1 PHD-H3K4me3 interaction and the importance of NuA3-dependent acetylation at K14. Furthermore, genome-wide ChIP-Chip analysis demonstrates colocalization of Yng1 and H3K4me3 in vivo. Disrupting the K4me3 binding of Yng1 altered K14ac and transcription at certain genes, thereby demonstrating direct in vivo evidence of sequential trimethyl binding, acetyltransferase activity, and gene regulation by NuA3. Our data support a general mechanism of transcriptional control through which histone acetylation upstream of gene activation is promoted partially through availability of H3K4me3, “read” by binding modules in select subunits.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2006.10.026