Ferrada Evandro
Center for Genomics and Bioinformatics, Faculty of Science, Universidad Mayor, Santiago, Chile.
Evol Bioinform Online. 2019 Aug 15;15:1176934319870485. doi: 10.1177/1176934319870485. eCollection 2019.
In order to preserve structure and function, proteins tend to preferentially conserve amino acids at particular sites along the sequence. Because mutations can affect structure and function, the question arises whether the preference of a protein site for a particular amino acid varies between protein homologs, and to what extent that variation depends on sequence divergence. Answering these questions can help in the development of models of sequence evolution, as well as provide insights on the dependence of the fitness effects of mutations on the genetic background of sequences, a phenomenon known as epistasis. Here, I comment on recent computational work providing a systematic analysis of the extent to which the amino acid preferences of proteins depend on the background mutations of protein homologs.
为了保持结构和功能，蛋白质倾向于优先保守序列中特定位置的氨基酸。由于突变会影响结构和功能，于是产生了这样一个问题：蛋白质位点对特定氨基酸的偏好性在蛋白质同源物之间是否存在差异，以及这种差异在多大程度上取决于序列分歧。回答这些问题有助于序列进化模型的开发，同时也能深入了解突变的适应性效应对序列遗传背景的依赖性，这一现象被称为上位性。在此，我对最近的计算工作进行评论，该工作对蛋白质的氨基酸偏好性在多大程度上依赖于蛋白质同源物的背景突变进行了系统分析。
