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Development of a DNA‐Templated Peptide Probe for Photoaffinity Labeling and Enrichment of the Histone Modification Reader Proteins
Author(s) -
Bai Xue,
Lu Congcong,
Jin Jin,
Tian Shanshan,
Guo Zhenchang,
Chen Pu,
Zhai Guijin,
Zheng Shuzhen,
He Xiwen,
Fan Enguo,
Zhang Yukui,
Zhang Kai
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201602558
Subject(s) - histone , computational biology , proteomics , photoaffinity labeling , chemistry , posttranslational modification , lysine , dna , histone h3 , peptide , biochemistry , microbiology and biotechnology , biology , gene , binding site , amino acid , enzyme
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.