Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlevskaya, Kazan, 420008, Russian Federation.
NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, 18 Kremlevskaya, Kazan, 420008, Russian Federation.
J Biomol NMR. 2019 May;73(5):223-227. doi: 10.1007/s10858-019-00254-4. Epub 2019 Jun 4.
Staphylococcus aureus hibernation promoting factor (SaHPF) is a 22,2 kDa protein which plays a crucial role in 100S Staphylococcus aureus ribosome formation during stress. SaHPF consists of N-terminal domain (NTD) that prevents proteins synthesis by binding to the 30S subunit at the P- and A-sites, connected through a flexible linker with a C-terminal domain (CTD) that keeps ribosomes in 100S form via homodimerization. Recently obtained 100S ribosome structure of S. aureus by cryo-EM shown that SaHPF-NTD bound to the ribosome active sites, however due to the absence of SaHPF-NTD structure it was modeled by homology with the E. coli hibernation factors HPF and YfiA. In present paper we have determined the solution structure of SaHPF-NTD by high-resolution NMR spectroscopy which allows us to increase structural knowledge about HPF structure from S. aureus.
金黄色葡萄球菌休眠促进因子（SaHPF）是一种 22.2 kDa 的蛋白质，在应激条件下，它在 100S 金黄色葡萄球菌核糖体形成中起着至关重要的作用。SaHPF 由 N 端结构域（NTD）组成，该结构域通过与 P 位和 A 位的 30S 亚基结合，阻止蛋白质合成，通过柔性接头与 C 端结构域（CTD）相连，CTD 通过同源二聚化使核糖体保持 100S 形式。最近通过 cryo-EM 获得的金黄色葡萄球菌 100S 核糖体结构表明，SaHPF-NTD 与核糖体活性位点结合，但由于 SaHPF-NTD 结构缺失，它通过与大肠杆菌休眠因子 HPF 和 YfiA 的同源性建模。在本研究中，我们通过高分辨率 NMR 光谱确定了 SaHPF-NTD 的溶液结构，这使我们能够增加对来自金黄色葡萄球菌的 HPF 结构的结构知识。
