Cell & Systems Biology, University of Toronto, 25 Harbord St., Toronto, ON M5S 3G5, Canada.
Cell & Systems Biology, University of Toronto, 25 Harbord St., Toronto, ON M5S 3G5, Canada. Electronic address: https://twitter.com/@taraneh_z.
Curr Opin Genet Dev. 2022 Oct;76:101964. doi: 10.1016/j.gde.2022.101964. Epub 2022 Aug 5.
Evolutionary preservation of protein structure had a major influence on the field of molecular evolution: changes in individual amino acids that did not disrupt protein folding would either have no effect or subtly change the 'lock' so that it could fit a new 'key'. Homology of individual amino acids could be confidently assigned through sequence alignments, and models of evolution could be tested. This view of molecular evolution excluded large regions of proteins that could not be confidently aligned, such as intrinsically disordered regions (IDRs) that do not fold into stable structures. In the last decade, major progress has been made in understanding the evolution of IDRs, much of it facilitated by new experimental and computational approaches in yeast. Here, we review this progress as well as several still outstanding questions.
不会破坏蛋白质折叠的单个氨基酸的变化要么没有影响，要么微妙地改变“锁”，使其能够适应新的“钥匙”。通过序列比对，可以有把握地分配个别氨基酸的同源性，并且可以测试进化模型。这种分子进化观点排除了无法有把握对齐的蛋白质的大片段，例如不能折叠成稳定结构的无规卷曲区域 (IDR)。在过去的十年中，在理解 IDR 的进化方面取得了重大进展，其中大部分得益于酵母中新的实验和计算方法。在这里，我们回顾这一进展以及几个仍然悬而未决的问题。
