Departamento de Quimica Fisica, Facultad de Ciencias, University of Granada, 18071 Granada, Spain.
Departamento de Quimica Fisica, Facultad de Ciencias, University of Granada, 18071 Granada, Spain.
Curr Opin Struct Biol. 2018 Aug;51:106-115. doi: 10.1016/j.sbi.2018.02.007. Epub 2018 Apr 13.
Approximations to the sequences of ancestral proteins can be derived from the sequences of their modern descendants. Proteins encoded by such reconstructed sequences can be prepared in the laboratory and subjected to experimental scrutiny. These 'resurrected' ancestral proteins often display remarkable properties, reflecting ancestral adaptations to intra-cellular and extra-cellular environments that differed from the environments hosting modern/extant proteins. Recent experimental and computational work has specifically discussed high stability, substrate and catalytic promiscuity, conformational flexibility/diversity and altered patterns of interaction with other sub-cellular components. In this review, we discuss these remarkable properties as well as recent attempts to explore their biotechnological and protein-engineering potential.
可以从现代后代的序列中推导出祖先蛋白质序列的近似值。可以在实验室中制备由这些重建序列编码的蛋白质，并对其进行实验研究。这些“复活”的祖先蛋白质通常表现出显著的特性，反映了祖先对与现代/现存蛋白质所处环境不同的细胞内和细胞外环境的适应。最近的实验和计算工作特别讨论了高稳定性、底物和催化的混杂性、构象的灵活性/多样性以及与其他细胞内成分相互作用模式的改变。在这篇综述中，我们讨论了这些显著的特性以及最近探索其生物技术和蛋白质工程潜力的尝试。
