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- W2912975650 abstract "Integration host factor (IHF) is an E.Coli architectural protein that exists as a heterodimer, composed of an α and β subunit. Originally identified in the integration of bacterial phage DNA, IHF has been implicated in regulating replication, transcription, recombination and nucleoid compaction. IHF binds to consensus sequences in the genome with high specificity and induces a bend of ∼160° in the DNA upon binding. This process helps package the genome and facilitate DNA protein interactions. Previous studies performed in our laboratory have shown that IHF binds to DNA four-way Holliday Junction with tight affinity and induces the junction to adopt the open conformation. In this study, we are interested in exploring the population distribution of different conformations of the DNA-junction complex using single-molecule Förster resonance energy transfer (FRET)system methodologies. To refine our single molecule methodologies for our system, our initial experiments are performed with 34 bp duplex DNA containing the IHF consensus sequence. Consistent with earlier studies, we find that IHF binds to consensus DNA with high affinity (3-10nM) and introduces a bend in the duplex DNA structure, as measured by steady state FRET. Preliminary data also show that we can observe IHF induced DNA bending event under the total internal reflection fluorescence (TIRF) spectroscopy. Our future work will focus on optimizing our conditions to perform similar measurements with the IHF-junction complex." @default.
- W2912975650 created "2019-02-21" @default.
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- W2912975650 date "2019-02-01" @default.
- W2912975650 modified "2023-09-30" @default.
- W2912975650 title "Establishing a Single-Molecule FRET System for Studying DNA-Protein Interactions" @default.
- W2912975650 doi "https://doi.org/10.1016/j.bpj.2018.11.2722" @default.
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