Protein-arginine Methyltransferase 1 (PRMT1) Methylates Ash2L, a Shared Component of Mammalian Histone H3K4 Methyltransferase Complexes
| Autor: | Cecilia Zurita-Lopez, Sharon Y.R. Dent, Mark T. Bedford, Jill Sergesketter Butler, Steven Clarke |
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| Rok vydání: | 2011 |
| Předmět: |
Protein-Arginine N-Methyltransferases
Methyltransferase Blotting Western Biology Methylation Biochemistry Cell Line Histone H1 Cell Line Tumor Histone methylation Histone H2A Humans Immunoprecipitation Histone code Gene Regulation Histone octamer Molecular Biology EZH2 Nuclear Proteins Histone-Lysine N-Methyltransferase Cell Biology DNA-Binding Proteins Repressor Proteins Histone methyltransferase Histone Methyltransferases Protein Processing Post-Translational HeLa Cells Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 286:12234-12244 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m110.202416 |
| Popis: | Multiple enzymes and enzymatic complexes coordinately regulate the addition and removal of post-translational modifications on histone proteins. The oncoprotein Ash2L is a component of the mixed lineage leukemia (MLL) family members 1-4, Setd1A, and Setd1B mammalian histone H3K4 methyltransferase complexes and is essential to maintain global trimethylation of histone H3K4. However, regulation of these complexes at the level of expression and activity remains poorly understood. In this report, we demonstrate that Ash2L is methylated on arginine residues both in vitro and in cells. We found that both protein-arginine methyltransferases 1 and 5 methylate Arg-296 within Ash2L. These findings are the first to demonstrate that post-translational modifications occur on the Ash2L protein and provide a novel example of cross-talk between chromatin-modifying enzyme complexes. |
| Databáze: | OpenAIRE |
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