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 Journal Article

   

Authors:	Taverna, S. D.; Ilin, S.; Rogers, R. S.; Tanny, J. C.; Lavender, H.; Li, H.; Baker, L.; Boyle, J.; Blair, L. P.; Chait, B. T.; Patel, D. J.; Aitchison, J. D.; Tackett, A. J.; Allis, C. D.
Article Title:	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
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. © 2006 Elsevier Inc. All rights reserved.
Keywords:	controlled study; methylation; promoter region; mutation; nonhuman; sensitivity and specificity; mass spectrometry; gene targeting; protein; protein binding; genetic transcription; transcription, genetic; enzyme activity; transcription factors; gene activation; dna; saccharomyces cerevisiae; chromatin immunoprecipitation; histone h3; nuclear magnetic resonance spectroscopy; models, molecular; saccharomyces cerevisiae proteins; histones; acetylation; gene activity; genome, fungal; nuclear magnetic resonance, biomolecular; open reading frames; promoter regions (genetics); histone acetyltransferase; histone acetyltransferases; protein yng1
Journal Title:	Molecular Cell
Volume:	24
Issue:	5
ISSN:	1097-2765
Publisher:	Cell Press
Date Published:	2006-12-08
Start Page:	785
End Page:	796
Language:	English
DOI:	10.1016/j.molcel.2006.10.026
PUBMED:	17157260
PROVIDER:	scopus
PMCID:	PMC4690528
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-33751527233&partnerID=40&md5=a9d091d3f8ecd24d1cf5d890b289361d
Notes:	--- - "Cited By (since 1996): 140" - "Export Date: 4 June 2012" - "CODEN: MOCEF" - "Source: Scopus"

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