期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 28, 页码 7993-7997出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201602558
关键词
epigenetics; histones; photo-crosslinking; protein modifications; proteomics
资金
- National Basic Research Program of China [2012CB910601, 2013CB910903]
- National Natural Science Foundation of China [21275077]
- Tianjin Municipal Science and Technology Commission [14JCYBJC24000]
Histone post-translational modifications (HPTMs) provide signal platforms to recruit proteins or protein complexes to regulate gene expression. Therefore, the identification of these recruited partners (readers) is essential to understand the underlying regulatory mechanisms. However, it is still a major challenge to profile these partners because their interactions with HPTMs are rather weak and highly dynamic. Herein we report the development of a HPTM dual probe based on DNA-templated technology and a photo-crosslinking method for the identification of HPTM readers. By using the trimethylation of histone H3 lysine 4, we demonstrated that this HPTM dual probe can be successfully utilized for labeling and enrichment of HPTM readers, as well as for the discovery of potential HPTM partners. This study describes the development of a new chemical proteomics tool for profiling HPTM readers and can be adapted for broad biomedical applications.
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