Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation
| Autor: | Kirmizis, Antonis, Santos-Rosa, H., Penkett, C. J., Singer, M. A., Vermeulen, M., Mann, M., Bähler, J., Green, R. D., Kouzarides, T. |
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| Přispěvatelé: | Kirmizis, Antonis [0000-0002-3748-8711] |
| Rok vydání: | 2007 |
| Předmět: |
arginine
mammal immunoprecipitation Shelterin Complex Euchromatin Histones Sirtuin 2 histone H3 Gene Expression Regulation Fungal Heterochromatin Histone methylation Sirtuins Silent Information Regulator Proteins Saccharomyces cerevisiae Epigenomics chromatin structure Multidisciplinary article Methylation protein function Chromatin unclassified drug DNA-Binding Proteins Biochemistry priority journal Histone methyltransferase Mammalia Genome Fungal DNA modification amino acid lipid storage Chromatin Immunoprecipitation Saccharomyces cerevisiae Proteins gene activation Genes Fungal Telomere-Binding Proteins Saccharomyces cerevisiae Biology Arginine lysine 4 Chromatin remodeling Histone Deacetylases Article protein modification Histone H3 Histone arginine methylation gene location nonhuman lysine Lysine genetic transcription heterochromatin protein subunit Histone-Lysine N-Methyltransferase DNA fungus antibody Protein Subunits enzyme Saccharomycetales gene expression methyltransferase methylation protein Transcription Factors |
| Zdroj: | Nature |
| Popis: | Modifications on histones control important biological processes through their effects on chromatin structure. Methylation at lysine 4 on histone H3 (H3K4) is found at the 5′ end of active genes and contributes to transcriptional activation by recruiting chromatin-remodelling enzymes. An adjacent arginine residue (H3R2) is also known to be asymmetrically dimethylated (H3R2me2a) in mammalian cells, but its location within genes and its function in transcription are unknown. Here we show that H3R2 is also methylated in budding yeast (Saccharomyces cerevisiae), and by using an antibody specific for H3R2me2a in a chromatin immunoprecipitation-on-chip analysis we determine the distribution of this modification on the entire yeast genome. We find that H3R2me2a is enriched throughout all heterochromatic loci and inactive euchromatic genes and is present at the 3′ end of moderately transcribed genes. In all cases the pattern of H3R2 methylation is mutually exclusive with the trimethyl form of H3K4 (H3K4me3). We show that methylation at H3R2 abrogates the trimethylation of H3K4 by the Set1 methyltransferase. The specific effect on H3K4me3 results from the occlusion of Spp1, a Set1 methyltransferase subunit necessary for trimethylation. Thus, the inability of Spp1 to recognize H3 methylated at R2 prevents Set1 from trimethylating H3K4. These results provide the first mechanistic insight into the function of arginine methylation on chromatin. ©2007 Nature Publishing Group. 449 928 932 Cited By :204 |
| Databáze: | OpenAIRE |
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