Wheeler Lucas C, Lim Shion A, Marqusee Susan, Harms Michael J
Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR, United States; Institute of Molecular Biology, University of Oregon, Eugene, OR, United States.
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, United States; Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA, United States.
Curr Opin Struct Biol. 2016 Jun;38:37-43. doi: 10.1016/j.sbi.2016.05.015. Epub 2016 Jun 9.
Were ancient proteins systematically different than modern proteins? The answer to this question is profoundly important, shaping how we understand the origins of protein biochemical, biophysical, and functional properties. Ancestral sequence reconstruction (ASR), a phylogenetic approach to infer the sequences of ancestral proteins, may reveal such trends. We discuss two proposed trends: a transition from higher to lower thermostability and a tendency for proteins to acquire higher specificity over time. We review the evidence for elevated ancestral thermostability and discuss its possible origins in a changing environmental temperature and/or reconstruction bias. We also conclude that there is, as yet, insufficient data to support a trend from promiscuity to specificity. Finally, we propose future work to understand these proposed evolutionary trends.
古代蛋白质与现代蛋白质在系统上存在差异吗？这个问题的答案至关重要，它塑造了我们理解蛋白质生化、生物物理和功能特性起源的方式。祖先序列重建（ASR）是一种推断祖先蛋白质序列的系统发育方法，可能会揭示出这样的趋势。我们讨论两种提出的趋势：从较高热稳定性到较低热稳定性的转变，以及蛋白质随着时间推移获得更高特异性的趋势。我们回顾了支持祖先热稳定性升高的证据，并讨论其在环境温度变化和/或重建偏差中的可能起源。我们还得出结论，目前尚无足够的数据支持从混杂性到特异性的趋势。最后，我们提出了未来的工作方向，以理解这些提出的进化趋势。
