INFN and Dipartimento di Fisica e Astronomia 'G. Galilei', Università di Padova, Via Marzolo 8, Padova, 35131, IT, Italy.
Dipartimento di Biomedicina Comparata e Alimentazione, Università di Padova, Viale dell' Università 16, Legnaro, 35020, IT, Italy.
Sci Rep. 2018 Jun 14;8(1):9141. doi: 10.1038/s41598-018-27287-3.
Proteins have coevolved with cellular environments to improve or preserve their functions, maintaining at the same time the degree of hydrophobicity necessary to fold correctly and enough solubility to perform their biological roles. Here, we study the Escherichia coli proteome using a Pareto front analysis in the solubility-hydrophobicity space. The results indicate the existence of a Pareto optimal front, a triangle whose vertices correspond to archetypal proteins specialized in distinct tasks, such as regulatory processes, membrane transport, outer-membrane pore formation, catalysis, and binding. The vertices are further enriched with proteins that occupy different subcellular compartments, namely, cytoplasmic, inner membrane, outer membrane, and outer membrane bounded periplasmic space. The combination of various enriching features offers an interpretation of how bacteria use the physico-chemical properties of proteins, both to drive them into their final destination in the cell and to have their tasks accomplished.
蛋白质与细胞环境共同进化，以改善或维持其功能，同时保持正确折叠所需的疏水性程度和足够的溶解度来发挥其生物学作用。在这里，我们使用 Pareto 前沿分析在溶解度-疏水性空间中研究大肠杆菌蛋白质组。结果表明存在 Pareto 最优前沿，一个三角形，其顶点对应于专门从事不同任务的典型蛋白质，如调节过程、膜运输、外膜孔形成、催化和结合。这些顶点进一步富集了占据不同亚细胞区室的蛋白质，即细胞质、内膜、外膜和外膜限定的周质空间。各种富集特征的结合提供了一种解释，说明细菌如何利用蛋白质的物理化学性质，将其驱入细胞内的最终目的地，并完成其任务。
