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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Carazo, José María Lázaro, Melisa Veprintsev, Dmitry B. Melero, Roberto Scheres, Sjors H. W. Valle, Mikel Rajagopalan, Sridharan Joerger, Andreas C. Fersht, Alan R. Lasso, Gorka Gil, David Brandt, Tobias |
| Description | Author Affiliation: Melero R ( Centro Nacional de Biotecnología, Darwin 3, 28049 Madrid, Spain.); |
| Abstract | The multidomain homotetrameric tumor suppressor p53 has two modes of binding dsDNA that are thought to be responsible for scanning and recognizing specific response elements (REs). The C termini bind nonspecifically to dsDNA. The four DNA-binding domains (DBDs) bind REs that have two symmetric 10 base-pair sequences. p53 bound to a 20-bp RE has the DBDs enveloping the DNA, which is in the center of the molecule surrounded by linker sequences to the tetramerization domain (Tet). We investigated by electron microscopy structures of p53 bound to DNA sequences consisting of a 20-bp RE with either 12 or 20 bp nonspecific extensions on either end. We found a variety of structures that give clues to recognition and scanning mechanisms. The 44- and 60-bp sequences gave rise to three and four classes of structures, respectively. One was similar to the known 20-bp structure, but the DBDs in the other classes were loosely arranged and incompatible with specific DNA recognition. Some of the complexes had density consistent with the C termini extending from Tet to the DNA, adjacent to the DBDs. Single-molecule fluorescence resonance energy transfer experiments detected the approach of the C termini towards the DBDs on addition of DNA. The structural data are consistent with p53 sliding along DNA via its C termini and the DNA-binding domains hopping on and off during searches for REs. The loose structures and posttranslational modifications account for the affinity of nonspecific DNA for p53 and point to a mechanism of enhancement of specificity by its binding to effector proteins. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 2 |
| Volume Number | 108 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2011-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | DNA Chemistry Microscopy, Electron Tumor Suppressor Protein P53 Alanine Cystine Fluorescence Resonance Energy Transfer Genes, P53 Mutation Nucleic Acid Conformation Protein Binding Protein Conformation Protein Structure, Quaternary Protein Structure, Tertiary 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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