Integration Host Factor: Putting a Twist on Protein–DNA Recognition
| Autor: | Aras N. Mattis, Thomas W Lynch, Erik K. Read, Jeffrey F. Gardner, Phoebe A. Rice |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
DNA
Bacterial Integration Host Factors Models Molecular Protein Conformation Mutant Protein dna Biology Crystallography X-Ray chemistry.chemical_compound Structural Biology Electrophoretic mobility shift assay Twist Binding site Base Pairing Molecular Biology Host factor Binding affinities Binding Sites Molecular biology biological factors Amino Acid Substitution chemistry Mutagenesis Biophysics bacteria DNA |
| Zdroj: | Journal of Molecular Biology. 330:493-502 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/s0022-2836(03)00529-1 |
| Popis: | Integration host factor (IHF) is a DNA–bending protein that recognizes its cognate sites through indirect readout. Previous studies have shown that binding of wild-type (WT)-IHF is disrupted by a T to A mutation at the center position of a conserved TTR motif in its binding site, and that substitution of βGlu44 with Ala prevented IHF from discriminating between A and T at this position. We have determined the crystal structures and relative binding affinities for all combinations of WT-IHF and IHF-βGlu44Ala bound to the WT and mutant DNAs. Comparison of these structures reveals that DNA twist plays a major role in DNA recognition by IHF, and that this geometric parameter is dependent on the dinucleotide step and not on the bound IHF variant. |
| Databáze: | OpenAIRE |
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