Photoaffinity labeling of transcription factors by DNA-templated crosslinking
Characterization of transcription factor-DNA interaction is of high importance in elucidating the molecular mechanisms of gene transcriptions. DNA-based affinity probes were developed to capture and identify transcription factors by covalent crosslinking; however, the requirement of a crosslinker on...
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| Veröffentlicht in: | Chemical science (Cambridge) 2015-01, Vol.6 (1), p.745-751 |
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| container_title | Chemical science (Cambridge) |
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| creator | Liu, Ying Zheng, Wenlu Zhang, Wan Chen, Nan Liu, Yang Chen, Li Zhou, Xiaozhou Chen, Xingshuo Zheng, Haifeng Li, Xiaoyu |
| description | Characterization of transcription factor-DNA interaction is of high importance in elucidating the molecular mechanisms of gene transcriptions. DNA-based affinity probes were developed to capture and identify transcription factors by covalent crosslinking; however, the requirement of a crosslinker on the affinity probe remains a disadvantage, as the crosslinker itself often interferes with the protein-DNA interactions. We report a dual-probe method able to capture DNA-binding transcription factors with unmodified protein-binding sites in scenarios where conventional probes have failed. We have also shown the method's converse application in selecting specific transcription factor-binding DNA sequences from a probe library and its extension to studying proteins recognizing epigenetic marks. This study may provide a new tool for exploring DNA-binding proteins in biology. |
| doi_str_mv | 10.1039/c4sc01953a |
| format | Article |
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DNA-based affinity probes were developed to capture and identify transcription factors by covalent crosslinking; however, the requirement of a crosslinker on the affinity probe remains a disadvantage, as the crosslinker itself often interferes with the protein-DNA interactions. We report a dual-probe method able to capture DNA-binding transcription factors with unmodified protein-binding sites in scenarios where conventional probes have failed. We have also shown the method's converse application in selecting specific transcription factor-binding DNA sequences from a probe library and its extension to studying proteins recognizing epigenetic marks. 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DNA-based affinity probes were developed to capture and identify transcription factors by covalent crosslinking; however, the requirement of a crosslinker on the affinity probe remains a disadvantage, as the crosslinker itself often interferes with the protein-DNA interactions. We report a dual-probe method able to capture DNA-binding transcription factors with unmodified protein-binding sites in scenarios where conventional probes have failed. We have also shown the method's converse application in selecting specific transcription factor-binding DNA sequences from a probe library and its extension to studying proteins recognizing epigenetic marks. 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| source | PubMed Central; DOAJ: Directory of Open Access Journals; EZB Electronic Journals Library; PubMed Central Open Access |
| subjects | Affinity Biology Chemistry Covalence Crosslinking Deoxyribonucleic acid Genes Proteins |
| title | Photoaffinity labeling of transcription factors by DNA-templated crosslinking |
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