Bach Institute of Biochemistry, Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia.
Int J Mol Sci. 2022 Mar 30;23(7):3816. doi: 10.3390/ijms23073816.
Protein-protein interactions (PPIs) play an important role in many biological processes in a living cell. Among them chaperone-client interactions are the most important. In this work PPIs of αB-crystallin and glycogen phosphorylase (Ph) in the presence of betaine (Bet) and arginine (Arg) at 48 °C and ionic strength of 0.15 M were studied using methods of dynamic light scattering, differential scanning calorimetry, and analytical ultracentrifugation. It was shown that Bet enhanced, while Arg reduced both the stability of αB-crystallin and its adsorption capacity (AC) to the target protein at the stage of aggregate growth. Thus, the anti-aggregation activity of αB-crystallin increased in the presence of Bet and decreased under the influence of Arg, which resulted in inhibition or acceleration of Ph aggregation, respectively. Our data show that chemical chaperones can influence the tertiary and quaternary structure of both the target protein and the protein chaperone. The presence of the substrate protein also affects the quaternary structure of αB-crystallin, causing its disassembly. This is inextricably linked to the anti-aggregation activity of αB-crystallin, which in turn affects its PPI with the target protein. Thus, our studies contribute to understanding the mechanism of interaction between chaperones and proteins.
蛋白质-蛋白质相互作用（PPIs）在活细胞的许多生物过程中起着重要作用。其中伴侣-客户相互作用是最重要的。在这项工作中，使用动态光散射、差示扫描量热法和分析超速离心法研究了在 48°C 和离子强度为 0.15 M 的条件下，甜菜碱（Bet）和精氨酸（Arg）存在时αB-晶体蛋白和糖原磷酸化酶（Ph）的 PPIs。结果表明，Bet 增强了αB-晶体蛋白的稳定性及其对目标蛋白在聚集体生长阶段的吸附能力（AC），而 Arg 则降低了αB-晶体蛋白的稳定性及其对目标蛋白的 AC。因此，在 Bet 的存在下，αB-晶体蛋白的抗聚集活性增加，而在 Arg 的影响下则降低，这分别导致 Ph 聚集的抑制或加速。我们的数据表明，化学伴侣可以影响目标蛋白和蛋白质伴侣的三级和四级结构。底物蛋白的存在也会影响αB-晶体蛋白的四级结构，导致其解体。这与αB-晶体蛋白的抗聚集活性密不可分，而抗聚集活性又会影响其与目标蛋白的 PPI。因此，我们的研究有助于理解伴侣蛋白与蛋白质相互作用的机制。
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