School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
Institute of Systems Biomedicine and Department of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
FEBS Open Bio. 2015 Mar 5;5:155-62. doi: 10.1016/j.fob.2015.02.006. eCollection 2015.
A great number of studies have proven that sHsps protect cells by inhibiting protein aggregation under heat stress, while little is known about their function to protect cells under acid stress. In this work, we show that Hsp20.1 and Hsp14.1 oligomers dissociated to smaller oligomeric species or even dimer/monomer at low pH (pH 4.0 and pH 2.0), whereas no prominent quaternary structural changes were seen at 50 °C. Both oligomers and smaller oligomeric species exhibited abilities to suppress client aggregation at low pH and at 50 °C. These results suggest that sHsps may function in different modes in different stressed conditions.
大量研究已经证明，在热应激条件下，小分子热休克蛋白通过抑制蛋白质聚集来保护细胞，而对于它们在酸性应激条件下保护细胞的功能知之甚少。在这项工作中，我们表明 Hsp20.1 和 Hsp14.1 寡聚体在低 pH 值（pH 4.0 和 pH 2.0）下解聚成较小的寡聚体甚至二聚体/单体，而在 50°C 时没有明显的四级结构变化。两种寡聚体和较小的寡聚体都具有在低 pH 值和 50°C 下抑制客户聚集的能力。这些结果表明，小分子热休克蛋白在不同的应激条件下可能以不同的模式发挥作用。
