期刊
NATURE CHEMICAL BIOLOGY
卷 12, 期 2, 页码 70-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1990
关键词
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资金
- Hong Kong Research Grants Council [GRF 17303114, GRF 17127915, HKU 709813P, CRF C7037-14G]
- University of Hong Kong [201411159101, 201409160027, 201311159007, 201309176090]
Post-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.
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