Parallel molecular mechanisms for enzyme temperature adaptation
Parallel molecular mechanisms for enzyme temperature adaptation
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DOI：
10.1126/science.aay2784
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发表时间：
2021-03-05
期刊：
影响因子：
56.9
通讯作者：
Herschlag, Daniel
中科院分区：
文献类型：
--
作者：
Pinney, Margaux M.;Mokhtari, Daniel A.;Herschlag, Daniel
酶的活性和稳定性对温度的适应机制是我们理解分子进化和酶如何工作的基础。在这里，我们研究酶温度适应的分子和进化机制，结合深入的机制研究和数千种酶的综合序列分析。我们发现，温度适应在甾酮异构酶（KSI）主要来自一个残基的变化与有限的，本地上位性，我们建立了潜在的物理机制。这种残基的变化发生在不同的KSI背景，表明平行适应温度。我们确定了1005个不同的细菌酶家族与生物体生长温度相关的残基，这表明广泛的平行适应温度。我们评估的残留物的性质，分子间的相互作用，和相互作用网络，似乎温度适应的基础。
The mechanisms that underly the adaptation of enzyme activities and stabilities to temperature are fundamental to our understanding of molecular evolution and how enzymes work. Here, we investigate the molecular and evolutionary mechanisms of enzyme temperature adaption, combining deep mechanistic studies with comprehensive sequence analyses of thousands of enzymes. We show that temperature adaptation in ketosteroid isomerase (KSI) arises primarily from one residue change with limited, local epistasis, and we establish the underlying physical mechanisms. This residue change occurs in diverse KSI backgrounds, suggesting parallel adaptation to temperature. We identify residues associated with organismal growth temperature across 1005 diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. We assess the residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation.