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Identification of Histone deacetylase (HDAC)-Associated Proteins with DNA-Programmed Affinity Labeling |
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| Authors: | Jianfu Zhang Jianzhao Peng Dr. Yiran Huang Ling Meng Qingrong Li Dr. Feng Xiong Prof. Xiaoyu Li |
| Affiliation: | 1. Department of Chemistry and the State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Laboratory for Synthetic Chemistry and Chemical Biology of Health@InnoHK, Pokfulam Road, Hong Kong SAR, China;2. Department of Chemistry and the State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Laboratory for Synthetic Chemistry and Chemical Biology of Health@InnoHK, Pokfulam Road, Hong Kong SAR, China Department of Chemistry, Southern University of Science and Technology China, 1088 Xueyuan Road, Shenzhen, China |
| Abstract: | Histone deacetylase (HDAC) is a major class of deacetylation enzymes. Many HDACs exist in large protein complexes in cells and their functions strongly depend on the complex composition. The identification of HDAC-associated proteins is highly important in understanding their molecular mechanisms. Although affinity probes have been developed to study HDACs, they were mostly targeting the direct binder HDAC, while other proteins in the complex remain underexplored. We report a DNA-based affinity labeling method capable of presenting different probe configurations without the need for preparing multiple probes. Using one binding probe, 9 probe configurations were created to profile HDAC complexes. Notably, this method identified indirect HDAC binders that may be inaccessible to traditional affinity probes, and it also revealed new biological implications for HDAC-associated proteins. This study provided a simple and broadly applicable method for characterizing protein-protein interactions. |
| Keywords: | affinity probes DNA-templated synthesis histone deacetylases photoaffinity labelling protein–protein interactions |