使用化学蛋白质组学策略对去乙酰化酶Sirtuin底物进行全球分析并通过荧光标记进行验证。
Global Profiling of Sirtuin Deacylase Substrates Using a Chemical Proteomic Strategy and Validation by Fluorescent Labeling.
作者信息
Zhang Shuai, Spiegelman Nicole A, Lin Hening
机构信息
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.
Department of Chemistry and Chemical Biology, Howard Hughes Medical Institute, Cornell University, Ithaca, NY, USA.
出版信息
Methods Mol Biol. 2019;2009:137-147. doi: 10.1007/978-1-4939-9532-5_11.
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.
蛋白质脂肪酰化是一种重要的翻译后修饰（PTM），并与许多基本生物学过程相关。据报道，沉默调节蛋白（sirtuins）是一类依赖烟酰胺腺嘌呤二核苷酸（NAD）的组蛋白去乙酰化酶，具有赖氨酸去脂肪酰化酶活性。对沉默调节蛋白进行全面的底物分析将有助于确定蛋白质赖氨酸脂肪酰化的功能及其受沉默调节蛋白的调控机制。在此，我们描述了一种用于全面分析沉默调节蛋白去脂肪酰化底物的化学蛋白质组学策略以及一种用于验证沉默调节蛋白底物的荧光标记方法。
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