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Chemoproteomic profiling unveils binding and functional diversity of endogenous proteins that interact with endogenous triplex DNA

nature Chemistry. 2024-09; 
Hongzhan Xu , Jing Ye # , Kui-Xing Zhang # , Qingxi Hu , Tongxiao Cui , Chong Tong , Mengqi Wang , Huichao Geng , Kun-Ming Shui , Yan Sun , Jian Wang , Xiaomeng Hou , Kai Zhang , Ran Xie , Yafei Yin , Nan Chen , Jia-Yu Chen
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Catalog Peptides G4 helicase assay was performed as previously described28,71 with minor modifications. Both intermolecular (OX-1 G4) and intramolecular (c-myc G4) G4 DNA were prepared as previously described28,72 and labelled with FAM (GenScript). Get A Quote

摘要

Triplex DNA structures, formed when a third DNA strand wraps around the major groove of DNA, are key molecular regulators and genomic threats. However, the regulatory network governing triplex DNA dynamics remains poorly understood. Here we reveal the binding and functional repertoire of proteins that interact with triplex DNA through chemoproteomic profiling in living cells. We develop a chemical probe that exhibits exceptional specificity towards triplex DNA. By employing a co-binding-mediated proximity capture strategy, we enrich triplex DNA interactome for quantitative proteomics analysis. This enables the identification of a comprehensive list of proteins that interact with triplex DNA, characterized by di... More

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