Linthwaite Victoria L, Cann Martin J
Department of Biosciences, Durham University, South Road, Durham DH1 3LE, UK.
Interface Focus. 2021 Apr 6;11(2):20200028. doi: 10.1098/rsfs.2020.0028. Epub 2021 Feb 12.
Carbon dioxide can influence cell phenotypes through the modulation of signalling pathways. CO regulates cellular processes as diverse as metabolism, cellular homeostasis, chemosensing and pathogenesis. This diversity of regulated processes suggests a broadly conserved mechanism for CO interactions with diverse cellular targets. CO is generally unreactive but can interact with neutral amines on protein under normal intracellular conditions to form a carbamate post-translational modification (PTM). We have previously demonstrated the presence of this PTM in a subset of protein produced by the model plant species . Here, we describe a detailed methodology for identifying new carbamate PTMs in an extracted soluble proteome under biologically relevant conditions. We apply this methodology to the soluble proteome of the model prokaryote and identify new carbamate PTMs The application of this methodology, therefore, supports the hypothesis that the carbamate PTM is both more widespread in biology than previously suspected and may represent a broadly relevant mechanism for CO-protein interactions.
二氧化碳可通过调节信号通路来影响细胞表型。一氧化碳调节多种细胞过程,如新陈代谢、细胞内稳态、化学传感和发病机制。这些受调节过程的多样性表明,一氧化碳与多种细胞靶点相互作用存在一种广泛保守的机制。一氧化碳通常不具反应性,但在正常细胞内条件下可与蛋白质上的中性胺相互作用,形成氨基甲酸盐翻译后修饰(PTM)。我们之前已证明在模式植物物种产生的一部分蛋白质中存在这种PTM。在此,我们描述了一种在生物学相关条件下,从提取的可溶性蛋白质组中鉴定新的氨基甲酸盐PTM的详细方法。我们将此方法应用于模式原核生物的可溶性蛋白质组,并鉴定出新的氨基甲酸盐PTM。因此,该方法的应用支持了这样一种假设,即氨基甲酸盐PTM在生物学中的分布比之前所怀疑的更为广泛,并且可能代表了一氧化碳与蛋白质相互作用的一种广泛相关机制。