Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 19, Pages 6522-6525Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b01431
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Funding
- National Natural Science Foundation of China [21521003, 21432002, 21572191]
- National Key Research and Development Program of China [2016YFA0501500]
- Hong Kong Research Grants Council [CRF C7029-15G, AoE/P-705/16, GRF 17303114, HKU 709813P]
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Posttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analogue that can be genetically and site-specifically incorporated into histone proteins. This, in conjunction with the genetically encoded photo-lysine as a control probe, enables the capture and identification of enzymatic machinery and/or effector proteins for histone lysine crotonylation.
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