Structure of the DNA-bound BRCA1 C-terminal Region from Human Replication Factor C p140 and Model of the Protein-DNA Complex
| Autor: | Kobayashi, M., AB, E., Bonvin, A.M.J.J., Siegal, G., NMR Spectroscopy, Dep Scheikunde, Sub NMR Spectroscopy |
|---|---|
| Přispěvatelé: | NMR Spectroscopy, Dep Scheikunde, Sub NMR Spectroscopy |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
DNA Replication
Magnetic Resonance Spectroscopy HMG-box Protein Conformation Molecular Sequence Data Eukaryotic DNA replication DNA and Chromosomes Biology Biochemistry DNA replication factor CDT1 Replication factor C Protein Interaction Mapping Humans Protein–DNA interaction Amino Acid Sequence Phosphorylation Replication Protein C Molecular Biology Sequence Homology Amino Acid BRCA1 Protein DNA replication Computational Biology DNA Cell Biology Molecular biology Protein Structure Tertiary Cell biology Kinetics BRCT domain biology.protein Origin recognition complex Algorithms |
| Zdroj: | Journal of Biological Chemistry, 285(13), 10087. American Society for Biochemistry and Molecular Biology Inc. Journal of Biological Chemistry Journal of Biological Chemistry, 285(13), 10087-10097 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m109.054106 |
| Popis: | BRCA1 C-terminal domain (BRCT)-containing proteins are found widely throughout the animal and bacteria kingdoms where they are exclusively involved in cell cycle regulation and DNA metabolism. Whereas most BRCT domains are involved in protein-protein interactions, a small subset has bona fide DNA binding activity. Here, we present the solution structure of the BRCT region of the large subunit of replication factor C bound to DNA and a model of the structure-specific complex with 5'-phosphorylated double-stranded DNA. The replication factor C BRCT domain possesses a large basic patch on one face, which includes residues that are structurally conserved and ligate the phosphate in phosphopeptide binding BRCT domains. An extra alpha-helix at the N terminus, which is required for DNA binding, inserts into the major groove and makes extensive contacts to the DNA backbone. The model of the protein-DNA complex suggests 5'-phosphate recognition by the BRCT domains of bacterial NAD(+)-dependent ligases and a nonclamp loading role for the replication factor C complex in DNA transactions. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|