Protein fatty-acylation is an important posttranslational modification (PTM) and has been associated with many fundamental biological processes. Sirtuins, the nicotinamide adenine dinucleotide (NAD)-dependent class of histone deacetylases have been reported to possess lysine defatty-acylase activity. Comprehensive substrate profiling of sirtuins will help to establish the function of both protein lysine fatty acylation and its regulation by sirtuins. Here, we describe a chemical proteomic strategy to globally profile sirtuin defatty-acylation substrates and a fluorescent labeling method to validate sirtuin substrates.
CITATION STYLE
Zhang, S., Spiegelman, N. A., & Lin, H. (2019). Global profiling of sirtuin deacylase substrates using a chemical proteomic strategy and validation by fluorescent labeling. In Methods in Molecular Biology (Vol. 2009, pp. 137–147). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9532-5_11
Mendeley helps you to discover research relevant for your work.