Evolution of protein specificity: insights from ancestral protein reconstruction.
Evolution of protein specificity: insights from ancestral protein reconstruction.
复制标题
蛋白质特异性的进化：来自祖先蛋白质重建的见解。
DOI：
10.1016/j.sbi.2017.07.003
复制
发表时间：
2017
影响因子：
6.8
通讯作者：
Thornton,JosephW
中科院分区：
文献类型：
--
作者：
Siddiq,MohammadA;Hochberg,GeorgKa;Thornton,JosephW
亮点祖先蛋白质重建揭示了分子相互作用是如何进化的。并非所有具有不同功能的旁系同源物都是从混杂的祖先进化而来的。一些特定的相互作用是通过非常简单的遗传机制从头进化而来的。静电互补性的变化驱动了特异性的进化。古代蛋白质并不比现代蛋白质更系统地混杂。蛋白质及其分子伴侣之间的特定相互作用驱动着大多数生物过程，因此了解这些相互作用如何进化是生物化学家和进化生物学家的一个重要问题。人们通常认为祖先蛋白质在系统上比现代蛋白质更加混杂，并且特异性通常在基因复制后通过划分和细化多功能祖先的活动而进化。然而，最近使用祖先蛋白质重建（APR）的研究发现，一些现代蛋白质家族中的配体特异性功能是从不具有这些功能的祖先那里从头进化而来的。此外，新的特异性相互作用是通过简单的机制进化而来的，只有少数突变改变了传统上公认的特异性生化决定因素，例如空间和静电互补性。因此，在进化过程中获得新的特定相互作用似乎既不困难也不罕见。相反，蛋白质很可能在进化过程中不断获得和失去新的活性，因为突变会导致相互作用界面的形状和静电发生微妙但随之而来的变化。然而，这些活动中只有少数被纳入有助于健康的生物过程中，然后它们就会因进一步突变的破坏而消失。
HighlightsAncestral protein reconstruction has revealed how molecular interactions evolved.Not all paralogs with distinct functions evolved from promiscuous ancestors.Some specific interactions evolved de novo by very simple genetic mechanisms.Changes in electrostatic complementarity have driven the evolution of specificity.Ancient proteins were not systematically more promiscuous than modern ones.Specific interactions between proteins and their molecular partners drive most biological processes, so understanding how these interactions evolve is an important question for biochemists and evolutionary biologists alike. It is often thought that ancestral proteins were systematically more promiscuous than modern proteins and that specificity usually evolves after gene duplication by partitioning and refining the activities of multifunctional ancestors. However, recent studies using ancestral protein reconstruction (APR) have found that ligand-specific functions in some modern protein families evolved de novo from ancestors that did not already have those functions. Further, the new specific interactions evolved by simple mechanisms, with just a few mutations changing classically recognized biochemical determinants of specificity, such as steric and electrostatic complementarity. Acquiring new specific interactions during evolution therefore appears to be neither difficult nor rare. Rather, it is likely that proteins continually gain and lose new activities over evolutionary time as mutations cause subtle but consequential changes in the shape and electrostatics of interaction interfaces. Only a few of these activities, however, are incorporated into the biological processes that contribute to fitness before they are lost to the ravages of further mutation.
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DOI：
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发表时间：
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影响因子：
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发表时间：
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影响因子：
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