European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Cambridge, UK.
Mol Syst Biol. 2013 Dec 22;9:714. doi: 10.1002/msb.201304521. Print 2013.
Protein post-translational modifications (PTMs) allow the cell to regulate protein activity and play a crucial role in the response to changes in external conditions or internal states. Advances in mass spectrometry now enable proteome wide characterization of PTMs and have revealed a broad functional role for a range of different types of modifications. Here we review advances in the study of the evolution and function of PTMs that were spurred by these technological improvements. We provide an overview of studies focusing on the origin and evolution of regulatory enzymes as well as the evolutionary dynamics of modification sites. Finally, we discuss different mechanisms of altering protein activity via post-translational regulation and progress made in the large-scale functional characterization of PTM function.
蛋白质翻译后修饰(PTMs)使细胞能够调节蛋白质活性,并在响应外部条件或内部状态变化方面发挥关键作用。 质谱技术的进步现在能够实现对 PTM 的全蛋白质组特征描述,并揭示了一系列不同类型修饰的广泛功能作用。 在这里,我们综述了这些技术进步所推动的 PTM 进化和功能研究方面的进展。 我们提供了一个综述,重点介绍了调节酶的起源和进化以及修饰位点的进化动态的研究。 最后,我们讨论了通过翻译后调控改变蛋白质活性的不同机制以及在 PTM 功能的大规模功能特征描述方面取得的进展。