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Chemoproteomic profiling unveils binding and functional diversity of endogenous proteins that interact with endogenous triplex DNA.
Xu, Hongzhan; Ye, Jing; Zhang, Kui-Xing; Hu, Qingxi; Cui, Tongxiao; Tong, Chong; Wang, Mengqi; Geng, Huichao; Shui, Kun-Ming; Sun, Yan; Wang, Jian; Hou, Xiaomeng; Zhang, Kai; Xie, Ran; Yin, Yafei; Chen, Nan; Chen, Jia-Yu.
Afiliación
  • Xu H; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Ye J; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Zhang KX; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Hu Q; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Cui T; State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Chemistry and Biomedicine Innovation Center, Nanjing University, Nanjing, China.
  • Tong C; Department of Cell Biology and Department of Cardiology of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
  • Wang M; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Geng H; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Shui KM; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Sun Y; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Wang J; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Hou X; ChomiX Biotech (Nanjing) Co. Ltd., Nanjing, China.
  • Zhang K; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China.
  • Xie R; State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Chemistry and Biomedicine Innovation Center, Nanjing University, Nanjing, China.
  • Yin Y; Department of Cell Biology and Department of Cardiology of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
  • Chen N; ChomiX Biotech (Nanjing) Co. Ltd., Nanjing, China.
  • Chen JY; State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Chemistry and Biomedicine Innovation Center, Department of Neurology, Nanjing Drum Tower Hospital, Nanjing University, Nanjing, China. jiayuchen@nju.edu.cn.
Nat Chem ; 2024 Sep 02.
Article en En | MEDLINE | ID: mdl-39223307
ABSTRACT
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 diverse binding properties and regulatory mechanisms in their native chromatin context. As a demonstration, we validate DDX3X as an ATP-independent triplex DNA helicase to unwind substrates with a 5' overhang to prevent DNA damage. Overall, our study provides a valuable resource for exploring the biology and translational potential of triplex DNA.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Nat Chem Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Nat Chem Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido