Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Vestec, Czech Republic.
Physiol Res. 2019 Apr 30;68(2):147-160. doi: 10.33549/physiolres.933950. Epub 2019 Jan 10.
Neutral trehalase 1 (Nth1) from Saccharomyces cerevisiae catalyzes disaccharide trehalose hydrolysis and helps yeast to survive adverse conditions, such as heat shock, starvation or oxidative stress. 14-3-3 proteins, master regulators of hundreds of partner proteins, participate in many key cellular processes. Nth1 is activated by phosphorylation followed by 14-3-3 protein (Bmh) binding. The activation mechanism is also potentiated by Ca(2+) binding within the EF-hand-like motif. This review summarizes the current knowledge about trehalases and the molecular and structural basis of Nth1 activation. The crystal structure of fully active Nth1 bound to 14-3-3 protein provided the first high-resolution view of a trehalase from a eukaryotic organism and showed 14-3-3 proteins as structural modulators and allosteric effectors of multi-domain binding partners.
中性海藻糖酶 1（Nth1）来自酿酒酵母，可催化二糖海藻糖水解，并帮助酵母在不利条件下生存，如热激、饥饿或氧化应激。14-3-3 蛋白是数百种伴侣蛋白的主要调控因子，参与许多关键的细胞过程。Nth1 通过磷酸化激活，然后与 14-3-3 蛋白（Bmh）结合。EF 手样模体中的 Ca（2+）结合也增强了激活机制。本综述总结了海藻糖酶的最新知识以及 Nth1 激活的分子和结构基础。与 14-3-3 蛋白结合的完全活性 Nth1 的晶体结构首次提供了来自真核生物的海藻糖酶的高分辨率视图，并显示 14-3-3 蛋白作为多结构域结合伴侣的结构调节剂和别构效应物。
