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...
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MDPI AG
2022-08-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/16/9497 |
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| author | Ho-Seong Jin Juyeon Son Yeo-Jin Seo Seo-Ree Choi Hye-Bin Ahn Youyeon Go Juhee Lim Kwang-Im Oh Kyoung-Seok Ryu Joon-Hwa Lee |
| author_facet | Ho-Seong Jin Juyeon Son Yeo-Jin Seo Seo-Ree Choi Hye-Bin Ahn Youyeon Go Juhee Lim Kwang-Im Oh Kyoung-Seok Ryu Joon-Hwa Lee |
| author_sort | Ho-Seong Jin |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-09T04:18:04Z |
| format | Article |
| id | doaj.art-83a304f773c141f2948982d6c8ec8b93 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T04:18:04Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-83a304f773c141f2948982d6c8ec8b932023-12-03T13:50:37ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-08-012316949710.3390/ijms23169497Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3Ho-Seong Jin0Juyeon Son1Yeo-Jin Seo2Seo-Ree Choi3Hye-Bin Ahn4Youyeon Go5Juhee Lim6Kwang-Im Oh7Kyoung-Seok Ryu8Joon-Hwa Lee9Department of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaProtein Structure Research Team, Korea Basic Science Institute, Ochang 28119, KoreaDepartment of Chemistry and RINS, Gyeongsang National University, Jinju 52828, KoreaDistal-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.https://www.mdpi.com/1422-0067/23/16/9497transcription factorNMRDNA–protein interactionsalt dependencebase-pair stabilitychemical shift perturbation |
| spellingShingle | Ho-Seong Jin Juyeon Son Yeo-Jin Seo Seo-Ree Choi Hye-Bin Ahn Youyeon Go Juhee Lim Kwang-Im Oh Kyoung-Seok Ryu Joon-Hwa Lee Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3 International Journal of Molecular Sciences transcription factor NMR DNA–protein interaction salt dependence base-pair stability chemical shift perturbation |
| title | Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3 |
| title_full | Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3 |
| title_fullStr | Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3 |
| title_full_unstemmed | Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3 |
| title_short | Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3 |
| title_sort | salt dependence of dna binding activity of human transcription factor dlx3 |
| topic | transcription factor NMR DNA–protein interaction salt dependence base-pair stability chemical shift perturbation |
| url | https://www.mdpi.com/1422-0067/23/16/9497 |
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