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ACS chemical biology v.12 no.1, 2017년, pp.57 - 62   SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry

Lu, Congcong (Department of Chemistry, Nankai University, Tianjin 300071, ); Tian, Shanshan (Tianjin Key Laboratory of Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin 300070, ); Zhai, Guijin (Tianjin Key Laboratory of Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin 300070, ); Yuan, Zuofei (Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, ); Li, Yijun (Department of Chemistry, Nankai University, Tianjin 300071, ); He, Xiwen (Department of Chemistry, Nankai University, Tianjin 300071, ); Zhang, Yukui (Department of Chemistry, Nankai University, Tianjin 300071, ); Zhang, Kai (Tianjin Key Laboratory of Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Department of Biochemistry and Molecular Biolo );
  • 초록  

    Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequence for specific recognition of histone H4, a biotin tag for affinity enrichment, an aryl azide photoactive group for cross-linking and a cleavable disulfide group to dissociate aptamer from labeled histones. We successfully achieved specific enrichment of histone H4 and further developed a new analysis strategy for histone-aptamer interaction by photo cross-linking mass spectrometry. The binding area of histone H4 to aptamer was investigated and discussed for the first time. This strategy exhibits great potential and might further contribute to the understanding of histone–DNA interaction patterns. Graphic Abstract ACS Electronic Supporting Info


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