The Tudor Tandem of 53BP1
| Autor: | Bernard Gilquin, Eric Quéméneur, Sophie Zinn-Justin, Isabelle Callebaut, Gaëlle Charier, Raphael Guerois, Béatrice Alpha-Bazin, Joël Couprie, Vincent Meyer |
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| Rok vydání: | 2004 |
| Předmět: |
0303 health sciences
Tudor domain HMG-box Kinetochore 030302 biochemistry & molecular biology Peptide binding G2-M DNA damage checkpoint Biology Molecular biology Cell biology 03 medical and health sciences chemistry.chemical_compound chemistry Structural Biology Helix Structural motif Molecular Biology DNA 030304 developmental biology |
| Zdroj: | Structure. 12:1551-1562 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2004.06.014 |
| Popis: | 53BP1 is a key transducer of the DNA damage checkpoint signal, which is required for phosphorylation of a subset of ATM substrates and p53 accumulation. After cell irradiation, the 53BP1 N-terminal region is phosphorylated. Its two C-terminal BRCT motifs interact with p53. Its central region is required and sufficient for 53BP1 foci formation at DNA strand breaks and for 53BP1 binding to the kinetochore. It contains an RG-rich segment and interacts with DNA in vitro. Here we show that the major globular domain of the 53BP1 central region adopts a new structural motif composed of two tightly packed Tudor domains and a C-terminal α helix. A unique surface essentially located on the first Tudor domain is involved in the binding to 53BP1 RG-rich sequence and to DNA, suggesting that the Tudor tandem can act as an adaptor mediating intramolecular as well as intermolecular protein-protein interactions and protein-nucleic acid associations. |
| Databáze: | OpenAIRE |
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