Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia, West Bengal, 741245, India.
Interdiscip Sci. 2018 Jun;10(2):390-399. doi: 10.1007/s12539-016-0199-y. Epub 2016 Nov 28.
Microbial oxidation-reduction reactions utilizing the environmental thiosulfate ions and mediated mainly by the sox operon are very much essential to maintain the sulfur balance in the environment. Majority of the previously documented wet laboratory studies show genetics behind the functionality of Sox proteins encoded by the sox operon. However, the molecular details of the involvements of the essential SoxB, SoxY and SoxZ proteins in the beta-proteobacteria have not yet been elucidated. In this work, an attempt was made to analyze the interaction profiles of the aforementioned SoxB, SoxY and SoxZ proteins to predict their roles in biological sulfur oxidation process. In order to establish the possible roles of these Sox proteins, we built the homology models of these proteins from the two different beta-proteobacteria Dechloromonas aromatica and Thiobacillus denitrificans. We then used molecular docking and simulation studies to further analyze the interaction profiles of these sox proteins. Our analyses revealed that SoxB protein from T. denitrificans exhibited steadier and stronger interactions with SoxYZ protein complex. On the other hand, SoxB protein from D. aromatica was found to exhibit a spontaneous interaction with greater ΔG values and therefore was well documented to exhibit a dual role. This is the first research article to discern the molecular level of interaction profiles of SoxB with SoxYZ protein complex in the beta-proteobacteria D. aromatica and T. denitrificans during the oxidations of thiosulfate. It would further prompt the future investigation into the mutational impact on the sequential interaction pattern in sox operon.
微生物氧化还原反应利用环境中的硫代硫酸盐离子,并主要由 sox 操纵子介导,对于维持环境中的硫平衡非常重要。大多数先前记录的实验室研究表明,sox 操纵子编码的 Sox 蛋白的功能背后存在遗传学。然而,β-变形菌中 SoxB、SoxY 和 SoxZ 蛋白参与的分子细节尚未阐明。在这项工作中,我们试图分析上述 SoxB、SoxY 和 SoxZ 蛋白的相互作用谱,以预测它们在生物硫氧化过程中的作用。为了确定这些 Sox 蛋白的可能作用,我们从两种不同的β-变形菌 Dechloromonas aromatica 和 Thiobacillus denitrificans 构建了这些蛋白质的同源模型。然后,我们使用分子对接和模拟研究进一步分析了这些 sox 蛋白的相互作用谱。我们的分析表明,来自 T. denitrificans 的 SoxB 蛋白与 SoxYZ 蛋白复合物表现出更稳定和更强的相互作用。另一方面,来自 D. aromatica 的 SoxB 蛋白被发现与 SoxYZ 蛋白复合物表现出自发的相互作用,具有更大的 ΔG 值,因此被很好地记录为具有双重作用。这是第一篇研究文章,它在β-变形菌 D. aromatica 和 T. denitrificans 中,区分了 SoxB 与 SoxYZ 蛋白复合物在硫代硫酸盐氧化过程中的分子水平相互作用谱。它将进一步促使未来对 sox 操纵子中连续相互作用模式的突变影响进行研究。