Carbon dioxide can influence cell phenotypes through the modulation of signalling pathways. CO₂ regulates cellular processes as diverse as metabolism, cellular homeostasis, chemosensing and pathogenesis. This diversity of regulated processes suggests a broadly conserved mechanism for CO₂ interactions with diverse cellular targets. CO₂ 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 Arabidopsis thaliana. 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 Escherichia coli 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 CO₂–protein interactions.

二氧化碳可以通过调节信号通路影响细胞表型。CO ₂调节多种细胞过程，如新陈代谢、细胞稳态、化学传感和发病机制。这种调节过程的多样性表明CO ₂与不同细胞靶标的相互作用具有广泛保守的机制。CO ₂通常不反应，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酯翻译后修饰 (PTM)。我们之前已经证明了这种 PTM 在由模式植物拟南芥产生的蛋白质子集中存在. 在这里，我们描述了一种详细的方法，用于在生物学相关条件下在提取的可溶性蛋白质组中识别新的氨基甲酸酯 PTM。我们将此方法应用于模型原核生物大肠杆菌的可溶性蛋白质组，并确定新的氨基甲酸酯 PTM 。_{因此，该方法的应用支持氨基甲酸酯 PTM 在生物学中比以前怀疑的更广泛并且可能代表与 CO 2}相互作用的广泛相关机制的假设。