PDF(Pubmed)
Abstract：
Post-translational modifications (PTMs) have been extensively studied in both eukaryotes and prokaryotes. Lysine acetylation, originally thought to be a rare occurrence in bacteria, is now recognized as a prevalent and important PTM in more than 50 species. This expansion in interest in bacterial PTMs became possible with the advancement of mass spectrometry technology and improved reagents such as acyl-modification specific antibodies. In this Review, we discuss how mass spectrometry-based proteomic studies of lysine acetylation and other acyl modifications have contributed to our understanding of bacterial physiology, focusing on recently published studies from 2018 to 2023. We begin with a discussion of approaches used to study bacterial PTMs. Next, we discuss newly characterized acylomes, including acetylomes, succinylomes, and malonylomes, in different bacterial species. In addition, we examine proteomic contributions to our understanding of bacterial virulence and biofilm formation. Finally, we discuss the contributions of mass spectrometry to our understanding of the mechanisms of acetylation, both enzymatic and nonenzymatic. We end with a discussion of the current state of the field and possible future research avenues to explore.
摘要：
翻译后修饰（PTM）已在真核生物和原核生物中得到广泛研究。赖氨酸乙酰化，最初被认为是细菌中罕见的，现在被认为是50多个物种中普遍存在和重要的PTM。随着质谱技术的进步和改进的试剂如酰基修饰特异性抗体,这种对细菌PTM的兴趣扩展成为可能。在这篇评论中,我们讨论了基于质谱的赖氨酸乙酰化和其他酰基修饰的蛋白质组学研究如何有助于我们对细菌生理学的理解，重点关注2018年至2023年最近发表的研究。我们首先讨论用于研究细菌PTM的方法。接下来，我们讨论新表征的酰基体，包括乙酰茎，琥珀酰胺,和丙二糖,在不同的细菌物种中。此外,我们研究了蛋白质组学对我们理解细菌毒力和生物膜形成的贡献。最后,我们讨论了质谱对我们理解乙酰化机理的贡献，酶和非酶。最后，我们讨论了该领域的现状以及未来可能的研究途径。
