Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 40, Pages 17525-17532Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202001205
Keywords
affinity probes; DNA-templated synthesis; histone deacetylases; photoaffinity labelling; protein-protein interactions
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Funding
- Research Grants Council of the Hong Kong SAR [AoE/P-705/16, 17321916, 17302817, 17301118, 17111319]
- National Natural Science Foundation of China [21572014, 21877093, 91953119]
- Laboratory for Synthetic Chemistry and Chemical Biology of Health@InnoHK of ITC, HKSAR
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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 configurationswithoutthe 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.
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