Methylation of Histone H3 Lys 4 in Coding Regions of Active Genes

Posttranslational modifications of histone tails regulate chromatin structure and transcription. Here we present global analyses of histone acetylation and histone H3 Lys 4 methylation patterns in yeast. We observe a significant correlation between acetylation of histones H3 and H4 in promoter regio...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2002-06, Vol.99 (13), p.8695-8700
Main Authors: Bernstein, Bradley E., Humphrey, Emily L., Erlich, Rachel L., Schneider, Robert, Bouman, Peter, Liu, Jun S., Kouzarides, Tony, Schreiber, Stuart L.
Format: Article
Language:English
Subjects:
Acetylation
Base Sequence
Biological Sciences
Cellular biology
Chromatin
Codes
Datasets
DNA
DNA Methylation
DNA Primers
Genes
Heterochromatin - metabolism
Histones
Histones - chemistry
Histones - metabolism
Lysine - metabolism
Methylation
Open reading frames
Promoter regions
Proteins
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Transcription, Genetic
Yeasts
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Summary:Posttranslational modifications of histone tails regulate chromatin structure and transcription. Here we present global analyses of histone acetylation and histone H3 Lys 4 methylation patterns in yeast. We observe a significant correlation between acetylation of histones H3 and H4 in promoter regions and transcriptional activity. In contrast, we find that dimethylation of histone H3 Lys 4 in coding regions correlates with transcriptional activity. The histone methyltransferase Set1 is required to maintain expression of these active, promoter-acetylated, and coding region-methylated genes. Global comparisons reveal that genomic regions deacetylated by the yeast enzymes Rpd3 and Hda1 overlap extensively with Lys 4 hypo- but not hypermethylated regions. In the context of recent studies showing that Lys 4 methylation precludes histone deacetylase recruitment, we conclude that Set1 facilitates transcription, in part, by protecting active coding regions from deacetylation.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.082249499