Protein adaptation to high hydrostatic pressure: Computational analysis of the structural proteome.

Proteins: Structure Pub Date : 2020-04-01 Epub Date: 2019-10-25 DOI:10.1002/prot.25839
Samvel Avagyan, Daniel Vasilchuk, George I Makhatadze
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引用次数: 4

Abstract

Hydrostatic pressure has a vital role in the biological adaptation of the piezophiles, organisms that live under high hydrostatic pressure. However, the mechanisms by which piezophiles are able to adapt their proteins to high hydrostatic pressure is not well understood. One proposed hypothesis is that the volume changes of unfolding (ΔVTot ) for proteins from piezophiles is distinct from those of nonpiezophilic organisms. Since ΔVTot defines pressure dependence of stability, we performed a comprehensive computational analysis of this property for proteins from piezophilic and nonpiezophilic organisms. In addition, we experimentally measured the ΔVTot of acylphosphatases and thioredoxins belonging to piezophilic and nonpiezophilic organisms. Based on this analysis we concluded that there is no difference in ΔVTot for proteins from piezophilic and nonpiezophilic organisms. Finally, we put forward the hypothesis that increased concentrations of osmolytes can provide a systemic increase in pressure stability of proteins from piezophilic organisms and provide experimental thermodynamic evidence in support of this hypothesis.

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蛋白质对高静水压的适应:结构蛋白质组的计算分析。
静水压对嗜压菌(生活在高静水压下的生物)的生物适应性起着至关重要的作用。然而,人们对嗜压生物使其蛋白质适应高静水压的机制还不甚了解。提出的一个假设是,嗜压菌蛋白质展开时的体积变化(ΔVTot)与非嗜压菌生物的不同。由于 ΔVTot 定义了稳定性的压力依赖性,我们对嗜压生物和非嗜压生物的蛋白质的这一特性进行了全面的计算分析。此外,我们还对嗜压生物和非嗜压生物的酰基磷酸酶和硫代毒素的 ΔVTot 进行了实验测量。根据这一分析,我们得出结论:嗜压生物和非嗜压生物的蛋白质在ΔVTot上没有差异。最后,我们提出了一个假设,即渗透溶质浓度的增加可系统性地提高嗜压生物蛋白质的压力稳定性,并提供了支持该假设的实验热力学证据。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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