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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Amigues, Béatrice Mousson, Florence Lautrette, Aurélie Agez, Morgane Ochsenbein, Françoise Thuret, Jean-yves Becker, Emmanuelle Neumann, Jean-michel Guerois, Raphaël Mann, Carl Courbeyrette, Régis |
| Description | Author Affiliation: Mousson F ( Service de Biophysique des Fonctions Membranaires and Service de Biochimie et de Génétique Moléculaire, Département de Biologie Joliot-Curie, Commissariat à l'Energie Atomique (CEA/Saclay), F-91191 Gif-sur-Yvette, France.); |
| Abstract | Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 17 |
| Volume Number | 102 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2005-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Cycle Proteins Chemistry Metabolism Histones Animals Binding Sites Glutathione Transferase Magnetic Resonance Spectroscopy Models, Molecular Mutagenesis, Site-Directed Protein Conformation Protein Structure, Secondary Recombinant Fusion Proteins Recombinant Proteins Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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