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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lu, Xiangdong Roeder, Robert G. Casadio, Fabio Garcia, Benjamin A. Allis, C. David Muir, Tom W. Leroy, Gary Pollock, Samuel B. |
| Description | Author Affiliation: Casadio F ( Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY 10065.); |
| Abstract | Histone posttranslational modification leads to downstream effects indirectly by allowing or preventing docking of effector molecules, or directly by changing the intrinsic biophysical properties of local chromatin. To date, little has been done to study posttranslational modifications that lie outside of the unstructured tail domains of histones. Core residues, and in particular arginines in H3 and H4, mediate key interactions between the histone octamer and DNA in forming the nucleosomal particle. Using mass spectrometry, we find that one of these core residues, arginine 42 of histone H3 (H3R42), is dimethylated in mammalian cells by the methyltransferases coactivator arginine methyltransferase 1 (CARM1) and protein arginine methyltransferase 6 (PRMT6) in vitro and in vivo, and we demonstrate that methylation of H3R42 stimulates transcription in vitro from chromatinized templates. Thus, H3R42 is a new, 'nontail' histone methylation site with positive effects on transcription. We propose that methylation of basic histone residues at the DNA interface may disrupt histone:DNA interactions, with effects on downstream processes, notably transcription. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 37 |
| Volume Number | 110 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2013-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Histones Chemistry Metabolism Nuclear Proteins Protein-Arginine N-Methyltransferases Amino Acid Sequence Animals Arginine Gene Knockdown Techniques HEK293 Cells HeLa Cells Genetics Methylation Mice Models, Molecular Molecular Sequence Data Antagonists & Inhibitors Protein Conformation Protein Processing, Post-Translational Transcription, Genetic Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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