Juyeon Son
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Juyeon Son has a total of 9 co-authors. Here are the top co-authors by number of shared publications:
- Ho-Seong Jin
Department of Chemistry and RINS, Gyeongsang National University, Jinju 52828, Korea
1 shared publication - Hye-Bin Ahn
Department of Chemistry and RINS, Gyeongsang National University, Jinju 52828, Korea
1 shared publication - Joon-Hwa Lee
Gyeongsang National University
1 shared publication - Juhee Lim
Department of Chemistry and RINS, Gyeongsang National University, Jinju 52828, Korea
1 shared publication - Kwang-Im Oh
Department of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea
1 shared publication - Kyoung-Seok Ryu
Korea Basic Science Institute
1 shared publication
Latest Publications
- Open Access
- 22 August 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (16) , 9497
Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3
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 α3 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.
- 22 August 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (16) , 9497
Open AccessSalt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3
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 α3 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.