中国科技核心期刊
CN:31-1600/Q
ISSN:1004-0374
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《生命科学》 2016, 28(4): 427-435
原核生物中蛋白质的赖氨酸乙酰化修饰
叶 青1, 2,王恩多1, 2, 3*
(1 中国科学院上海生命科学研究院生物化学与细胞生物学研究所,分子细胞科学卓越创新中心,分子生物学国家重点实验室,上海 200031;2 中国科学院大学,北京 100049;3 上海科技大学,上海 200031)
摘 要:翻译后修饰(post-translational modification, PTM) 可以调节蛋白质的结构、稳定性和功能。作为一种PTM,赖氨酸乙酰化修饰被发现存在于三界生物中,参与了包括中心代谢、转录调控、蛋白质合成、细胞形态、细胞周期、信号通路调控、应激反应、病原微生物感染调控等多个重要的生理学进程。近年来,高分辨率质谱、高亲和泛乙酰化蛋白抗体的富集纯化等多种技术的发展和运用逐渐揭开了原核生物中蛋白质乙酰化修饰的面纱。乙酰化修饰在原核生物中广泛存在,且起着功能调控的作用。现简要介绍蛋白质乙酰化修饰的研究历史和原核生物中乙酰化修饰的调节机制,并重点总结若干已有具体研究的乙酰化修饰蛋白质,探讨原核生物蛋白质乙酰化修饰研究中今后需要解决的问题。
 
Lysine acetylation of proteins in prokaryotes
YE Qing1, 2, WANG En-Duo1, 2, 3*
(1 State Key Laboratory of Molecular Biology, Chinese Academy of Sciences Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; 2 University of Chinese Academy of Sciences, Beijing 100049, China; 3 ShanghaiTech University, Shanghai 200031, China)
Abstract: Post-translational modifications (PTM) are essential to proteins in many ways, including improvement of stability, correct folding and regulation of functions. Lysine acetylation, as one kind of PTMs found in three domains of life, implicates in multiple cellular processes including central metabolism, transcription, translation, cell morphology, cell cycle, signal transduction, stress response and the infection of pathogenic microorganism. Though studies about acetylation mainly focus on eukaryotes, with the development and application of techniques like high-resolution mass spectrometry and generation of high-affinity pan-acetylation protein antibody, more evidence has shown that in prokaryotes a variety of proteins are acetylated and some of them are functionally regulated by this kind of modification. In this review, we would bring together the history and latest findings of acetylation in prokaryotes and highlight several well-studied examples in various species. In addition, we would like to raise several interesting questions to shed light on the future directions of research.
 
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