| G9a-mediated lysine methylation alters the function of CCAAT/enhancer-binding protein-beta. | |
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MedLine Citation:
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PMID: 18647749 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The functional capacity of the transcriptional regulatory CCAAT/enhancer-binding protein-beta (C/EBPbeta) is governed by protein interactions and post-translational protein modifications. In a proteome-wide interaction screen, the histone-lysine N-methyltransferase, H3 lysine 9-specific 3 (G9a), was found to directly interact with the C/EBPbeta transactivation domain (TAD). Binding between G9a and C/EBPbeta was confirmed by glutathione S-transferase pulldown and co-immunoprecipitation. Metabolic labeling showed that C/EBPbeta is post-translationally modified by methylation in vivo. A conserved lysine residue in the C/EBPbeta TAD served as a substrate for G9a-mediated methylation. G9a, but not a methyltransferase-defective G9a mutant, abrogated the transactivation potential of wild type C/EBPbeta. A C/EBPbeta TAD mutant that contained a lysine-to-alanine exchange was resistant to G9a-mediated inhibition. Moreover, the same mutation conferred super-activation of a chromatin-embedded, endogenous C/EBPbeta target gene. Our data identify C/EBPbeta as a direct substrate of G9a-mediated post-translational modification that alters the functional properties of C/EBPbeta during gene regulation. |
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Authors:
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Ole Pless; Elisabeth Kowenz-Leutz; Maria Knoblich; Jörn Lausen; Michael Beyermann; Martin J Walsh; Achim Leutz |
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Publication Detail:
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Type: Journal Article Date: 2008-07-21 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 283 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2008 Sep |
Date Detail:
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Created Date: 2008-09-22 Completed Date: 2008-11-10 Revised Date: 2012-01-18 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 26357-63 Citation Subset: IM |
Affiliation:
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Max Delbrück Center for Molecular Medicine, Humboldt University of Berlin, Berlin, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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CCAAT-Enhancer-Binding Protein-beta
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genetics,
metabolism* HeLa Cells Histocompatibility Antigens / genetics, metabolism* Histone-Lysine N-Methyltransferase / genetics, metabolism* Humans Mutation Protein Processing, Post-Translational / physiology* Protein Structure, Tertiary / physiology Proteome / genetics, metabolism* Transcriptional Activation / physiology* |
| Chemical | |
Reg. No./Substance:
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0/CCAAT-Enhancer-Binding Protein-beta; 0/Histocompatibility Antigens; 0/Proteome; EC 2.1.1.43/EHMT2 protein, human; EC 2.1.1.43/Histone-Lysine N-Methyltransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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