Abstract:
: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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Taverna SD,Ilin S,Rogers RS,Tanny JC,Lavender H,Li H,Baker L,Boyle J,Blair LP,Chait BT,Patel DJ,Aitchison JD,Tackett AJ,Allis CDdoi
10.1016/j.molcel.2006.10.026subject
Has Abstractpub_date
2006-12-08 00:00:00pages
785-796issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(06)00732-5journal_volume
24pub_type
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