Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3open access
- Jin, Ho-Seong; Son, Juyeon; Seo, Yeo-Jin; Choi, Seo-Ree; Ahn, Hye-Bin; Go, Youyeon; Lim, Juhee; Oh, Kwang-Im; Ryu, Kyoung-Seok; Lee, Joon-Hwa
- Issue Date
- transcription factor; NMR; DNA-protein interaction; salt dependence; base-pair stability; chemical shift perturbation
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.23, no.16
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Distal-less 3 (Dlx3) is a homeobox-containing transcription factor and plays a crucial role in the development and differentiation process. Human Dlx3 consists of two transactivation domains and a homeobox domain (HD) that selectively binds to the consensus site (5 '-TAATT-3 ') of the DNA duplex. Here, we performed chemical shift perturbation experiments on Dlx3-HD in a complex with a 10-base-paired (10-bp) DNA duplex under various salt conditions. We also acquired the imino proton spectra of the 10-bp DNA to monitor the changes in base-pair stabilities during titration with Dlx3-HD. Our study demonstrates that Dlx3-HD selectively recognizes its consensus DNA sequences through the alpha 3 helix and L1 loop regions with a unique dynamic feature. The dynamic properties of the binding of Dlx3-HD to its consensus DNA sequence can be modulated by varying the salt concentrations. Our study suggested that this unique structural and dynamic feature of Dlx3-HD plays an important role in target DNA recognition, which might be associated with tricho-dento-osseous syndrome.
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- 자연과학대학 > 화학과 > Journal Articles
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