Methylation of histone H3 Lys 4 in coding regions of active genes
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- 11 June 2002
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 99 (13) , 8695-8700
- https://doi.org/10.1073/pnas.082249499
Abstract
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.Keywords
This publication has 42 references indexed in Scilit:
- 25 years after the nucleosome model: chromatin modificationsTrends in Biochemical Sciences, 2000
- Effects of Histone Tail Domains on the Rate of Transcriptional Elongation through a NucleosomeMolecular and Cellular Biology, 2000
- Genomewide studies of histone deacetylase function in yeastProceedings of the National Academy of Sciences, 2000
- Global histone acetylation and deacetylation in yeastNature, 2000
- Histone acetylation and an epigenetic codeBioEssays, 2000
- Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylaseNature, 2000
- Signaling and Circuitry of Multiple MAPK Pathways Revealed by a Matrix of Global Gene Expression ProfilesScience, 2000
- Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in TetrahymenaProceedings of the National Academy of Sciences, 1999
- In Vivo Cross-Linking and Immunoprecipitation for Studying Dynamic Protein:DNA Associations in a Chromatin EnvironmentMethods, 1999
- Exploring the Metabolic and Genetic Control of Gene Expression on a Genomic ScaleScience, 1997