Identification of Acetylated Proteins in Borrelia burgdorferi.
Identification of Acetylated Proteins in Borrelia burgdorferi.
复制标题
伯氏疏螺旋体中乙酰化蛋白的鉴定。
DOI：
10.1007/978-1-4939-7383-5_14
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Yang,XFrank
中科院分区：
文献类型：
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作者：
Yang,Youyun;Wolfe,Alan;Yang,XFrank
蛋白质的翻译后修饰(PTM)已经成为生命三个领域中的一种主要调节机制。一种新兴的Ptm是Nε-赖氨酸乙酰化-赖氨酸残基的epsilon氨基的乙酰化。N-ε-赖氨酸乙酰化被认为可以调节多种细胞过程。在真核生物中，它调节染色质结构、转录、代谢、信号转导和细胞骨架。最近，多个小组在不同的细菌门中检测到N-ε-赖氨酸乙酰化，但关于伯氏疏螺旋体蛋白乙酰化的研究尚未见报道。在这里，我们描述了一种循序渐进的方法来鉴定Nε-赖氨酸乙酰化蛋白INB。勃格多费里。
Posttranslational modification (PTM) of proteins has emerged as a major regulatory mechanism in all three domains of life. One emerging PTM is Nε-lysine acetylation—the acetylation of the epsilon amino group of lysine residues. Nε-lysine acetylation is known to regulate multiple cellular processes. In eukaryotes, it regulates chromatin structure, transcription, metabolism, signal transduction, and the cytoskeleton. Recently, multiple groups have detected Nε-lysine acetylation in diverse bacterial phyla, but no work on protein acetylation inBorrelia burgdorferihas been reported. Here, we describe a step-by-step protocol to identify Nε-lysine acetylated proteins inB. burgdorferi.