Univ. Bourgogne Franche-comté, AgroSup Dijon, PAM UMR A 02.102, Dijon, France.
Cell Stress Chaperones. 2023 Jan;28(1):21-33. doi: 10.1007/s12192-022-01308-7. Epub 2022 Nov 11.
Several strategies have been put in place by organisms to adapt to their environment. One of these strategies is the production of stress proteins such as sHSPs, which have been widely described over the last 30 years for their role as molecular chaperones. Some sHSPs have, in addition, the particularity to exert a lipochaperone role by interacting with membrane lipids to maintain an optimal membrane fluidity. However, the mechanisms involved in this sHSP-lipid interaction remain poorly understood and described rather sporadically in the literature. This review gathers the information concerning the structure and function of these proteins available in the literature in order to highlight the mechanism involved in this interaction. In addition, analysis of primary sequence data of sHSPs available in database shows that sHSPs can interact with lipids via certain amino acid residues present on some β sheets of these proteins. These residues could have a key role in the structure and/or oligomerization dynamics of sHPSs, which is certainly essential for interaction with membrane lipids and consequently for maintaining optimal cell membrane fluidity.
生物体已经采取了几种策略来适应环境。其中一种策略是产生应激蛋白，如 sHSPs，它们在过去 30 年中因其作为分子伴侣的作用而被广泛描述。一些 sHSPs 还具有通过与膜脂相互作用来维持最佳膜流动性的脂伴侣的特殊性。然而，这种 sHSP-脂质相互作用的机制仍知之甚少，在文献中也只是零星描述。这篇综述汇集了文献中关于这些蛋白质结构和功能的信息，以强调这种相互作用所涉及的机制。此外，对数据库中 sHSPs 的一级序列数据的分析表明，sHSPs 可以通过这些蛋白质某些 β 片层上的某些氨基酸残基与脂质相互作用。这些残基可能在 sHPSs 的结构和/或寡聚动力学中起关键作用，这对于与膜脂相互作用以及维持最佳细胞膜流动性肯定是必不可少的。
