Histone H2A Monoubiquitination Represses Transcription by Inhibiting RNA Polymerase II Transcriptional Elongation
Solving the biological roles of covalent histone modifications, including monoubiquitination of histone H2A, and the molecular mechanisms by which these modifications regulate specific transcriptional programs remains a central question for all eukaryotes. Here we report that the N-CoR/HDAC1/3 compl...
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| Veröffentlicht in: | Molecular cell 2008-01, Vol.29 (1), p.69-80 |
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| creator | Zhou, Wenlai Zhu, Ping Wang, Jianxun Pascual, Gabriel Ohgi, Kenneth A. Lozach, Jean Glass, Christopher K. Rosenfeld, Michael G. |
| description | Solving the biological roles of covalent histone modifications, including monoubiquitination of histone H2A, and the molecular mechanisms by which these modifications regulate specific transcriptional programs remains a central question for all eukaryotes. Here we report that the N-CoR/HDAC1/3 complex specifically recruits a specific histone H2A ubiquitin ligase, 2A-HUB/hRUL138, to a subset of regulated gene promoters. 2A-HUB catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for specific gene regulation programs. Thus, 2A-HUB mediates a selective repression of a specific set of chemokine genes in macrophages, critically modulating migratory responses to TLR activation. H2A monoubiquitination acts to prevent FACT recruitment at the transcriptional promoter region, blocking RNA polymerase II release at the early stage of elongation. We suggest that distinct H2A ubiquitinases, each recruited based on interactions with different corepressor complexes, contribute to distinct transcriptional repression programs. |
| doi_str_mv | 10.1016/j.molcel.2007.11.002 |
| format | Article |
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Here we report that the N-CoR/HDAC1/3 complex specifically recruits a specific histone H2A ubiquitin ligase, 2A-HUB/hRUL138, to a subset of regulated gene promoters. 2A-HUB catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for specific gene regulation programs. Thus, 2A-HUB mediates a selective repression of a specific set of chemokine genes in macrophages, critically modulating migratory responses to TLR activation. H2A monoubiquitination acts to prevent FACT recruitment at the transcriptional promoter region, blocking RNA polymerase II release at the early stage of elongation. 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| ispartof | Molecular cell, 2008-01, Vol.29 (1), p.69-80 |
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| subjects | Amino Acid Sequence Animals Cell Line Chemokines - biosynthesis Chemokines - genetics DNA DNA-Binding Proteins - antagonists & inhibitors DNA-Binding Proteins - physiology High Mobility Group Proteins - antagonists & inhibitors Histone Deacetylase 1 Histone Deacetylases - physiology Histones - metabolism Humans Ligases - chemistry Ligases - physiology Macrophages - metabolism Mice Molecular Sequence Data Nuclear Proteins - physiology Nuclear Receptor Co-Repressor 1 Nuclear Receptor Co-Repressor 2 Peptide Chain Elongation, Translational - genetics Protein Processing, Post-Translational - genetics PROTEINS Repressor Proteins - chemistry Repressor Proteins - physiology RING Finger Domains RNA Polymerase II - antagonists & inhibitors RNA-Binding Proteins - chemistry RNA-Binding Proteins - physiology Transcription, Genetic - genetics Transcriptional Elongation Factors - antagonists & inhibitors Ubiquitin - metabolism Ubiquitin-Protein Ligases Ubiquitination - genetics |
| title | Histone H2A Monoubiquitination Represses Transcription by Inhibiting RNA Polymerase II Transcriptional Elongation |
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