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Glutamine methylation in histone H2A is an RNA -polymerase -1 - dedicated modification

机译：组蛋白H2A中的谷氨酰胺甲基化是RNA-聚合酶-1-专用修饰

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摘要

Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here we describe a new class of histone modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nopl as the methyltransferase in yeast and demonstrate that fibrillarin is the orthologue enzyme in human cells. Glutamine methylation of H2A is restricted to the nudeolus. Global analysis in yeast, using an H2AQ105me-specific antibody, shows that this modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (facilitator of chromatin transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 shows reduced histone incorporation and increased transcription at the ribosomal DNA locus. These features are phenocopied by mutations in FACT complex components. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.
机译：核小体修饰有许多能够影响许多DNA过程的翻译后修饰。在这里，我们描述了一类新的组蛋白修饰，即谷氨酰胺的甲基化，发生在酵母组蛋白H2A的位置105（Q105）和人H2A的Q104处。我们确定Nopl为酵母中的甲基转移酶，并证明原纤维蛋白是人类细胞中的直向同源酶。 H2A的谷氨酰胺甲基化仅限于裸核。使用H2AQ105me特异性抗体对酵母进行的全局分析表明，这种修饰仅富集于35S核糖体DNA转录单位上。我们显示，Q105残基是组蛋白伴侣FACT（染色质转录的促进子）复合物结合位点的一部分。 Q105的甲基化或其取代为丙氨酸会在体外破坏与FACT的结合。在Q105突变的酵母菌株显示出减少的组蛋白掺入和在核糖体DNA基因座处的转录增加。这些功能通过FACT复杂组件中的突变表现出来。这些数据一起将H2A的谷氨酰胺甲基化识别为专用于特定RNA聚合酶的第一个组蛋白表观遗传标记，并定义了其作为FACT与核小体相互作用的调节剂的功能。

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  • 来源
    《Nature》 |2014年第7484期|564-568|共5页
  • 作者

    Peter Tessarz; Helena Santos-Rosa; Sam C. Robson; Kathrine B. Sylvestersen; Christopher J. Nelson; Michael L. Nielsen; Tony Kouzarides;

  • 作者单位

    Gurdon Institute, University ot Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK,Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK;

    Gurdon Institute, University ot Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK,Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK;

    Gurdon Institute, University ot Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK,Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK;

    Department of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark;

    Gurdon Institute, University ot Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK,Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK,Department of Biochemistry and Microbiology, University of Victoria, 3800 Finnerty Road, Victoria, British Columbia V8P 5C2, Canada;

    Department of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark;

    Gurdon Institute, University ot Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK,Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK;

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