CEA, iBiTecS, F-91191 Gif sur Yvette, France; Université Paris-Sud & CNRS, UMR 8221, F-91191 Gif sur Yvette, France.
Arch Biochem Biophys. 2014 Jul 15;554:65-75. doi: 10.1016/j.abb.2014.05.010. Epub 2014 May 20.
Protein-protein interactions lie at the heart of most cellular processes. Many experimental and computational studies aim to deepen our understanding of these interactions and improve our capacity to predict them. In this respect, the evolutionary perspective is most interesting, since the preservation of structure and function puts constraints on the evolution of proteins and their interactions. However, uncovering these constraints remains a challenge, and the description and detection of evolutionary signals in protein-protein interactions is currently a very active field of research. Here, we review recent works dissecting the mechanisms of protein-protein interaction evolution and exploring how to use evolutionary information to predict interactions, both at the global level of the interactome and at the detailed level of protein-protein interfaces. We first present to what extent protein-protein interactions are found to be conserved within interactomes and which properties can influence their conservation. We then discuss the evolutionary and co-evolutionary pressures applied on protein-protein interfaces. Finally, we describe how the computational prediction of interfaces can benefit from evolutionary inputs.
蛋白质-蛋白质相互作用是大多数细胞过程的核心。许多实验和计算研究旨在加深我们对这些相互作用的理解，并提高我们预测它们的能力。在这方面，进化的观点是最有趣的，因为结构和功能的保存对蛋白质及其相互作用的进化施加了限制。然而，揭示这些限制仍然是一个挑战，描述和检测蛋白质-蛋白质相互作用中的进化信号目前是一个非常活跃的研究领域。在这里，我们回顾了最近的研究工作，这些工作剖析了蛋白质-蛋白质相互作用进化的机制，并探讨了如何利用进化信息来预测相互作用，包括在互作组的全局水平和蛋白质-蛋白质界面的详细水平。我们首先介绍了在多大程度上发现蛋白质-蛋白质相互作用在互作组内是保守的，以及哪些特性可以影响它们的保守性。然后，我们讨论了蛋白质-蛋白质界面上施加的进化和共进化压力。最后，我们描述了如何从进化输入中受益于界面的计算预测。
