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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Yi, Gwan-su Lu, Ying Liao, Jack C. C. Pineda-lucena, Antonio Kaustov, Lilia Bochkarev, Alexey Arrowsmith, Cheryl H. Ayed, Ayeda Okorokov, Andrei L. Bochkareva, Elena Milner, Jo |
Description | Author Affiliation: Bochkareva E ( Banting and Best Department of Medical Research & Department of Medical Genetics and Microbiology, University of Toronto, 112 College Street, Toronto, Ontario, Canada M5G 1L6.); |
Abstract | One of many protein-protein interactions modulated upon DNA damage is that of the single-stranded DNA-binding protein, replication protein A (RPA), with the p53 tumor suppressor. Here we report the crystal structure of RPA residues 1-120 (RPA70N) bound to the N-terminal transactivation domain of p53 (residues 37-57; p53N) and, by using NMR spectroscopy, characterize two mechanisms by which the RPA/p53 interaction can be modulated. RPA70N forms an oligonucleotide/oligosaccharide-binding fold, similar to that previously observed for the ssDNA-binding domains of RPA. In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N. The H2 helix of p53 structurally mimics the binding of ssDNA to the oligonucleotide/oligosaccharide-binding fold. NMR experiments confirmed that both ssDNA and an acidic peptide mimicking a phosphorylated form of RPA32N can independently compete the acidic p53N out of the binding site. Taken together, our data suggest a mechanism for DNA damage signaling that can explain a threshold response to DNA damage. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 43 |
Volume Number | 102 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 2005-10-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | DNA, Single-Stranded Chemistry Replication Protein A Transcriptional Activation Tumor Suppressor Protein P53 Amino Acid Sequence Binding Sites Binding, Competitive DNA Damage Molecular Sequence Data Phosphorylation Protein Folding Protein Structure, Tertiary Metabolism Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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