Chair of Biomolecular NMR Spectroscopy, Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.
Chair of Biomolecular NMR Spectroscopy, Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, 85764 Neuherberg, Germany.
FEBS Lett. 2014 May 2;588(9):1755-66. doi: 10.1016/j.febslet.2014.03.031. Epub 2014 Apr 3.
The conserved C-terminal FATC domain of the kinase 'target of rapamycin' is important for its regulation and was suggested to contain a peripheral membrane anchor. Here, we present the characterization of the interactions of the yeast TOR1 FATC domain (2438-2470=y1fatc) and 15 mutants with membrane mimetic micelles, bicelles, and small unilamellar vesicles (SUVs) by NMR and CD spectroscopy. Replacement of up to 6-7 residues did not result in a significant abrogation of the association with micelles or bicelles. However, replacement of only one residue could result in an impairment of the interaction with SUVs that are usually used at low concentrations. Some mutants not binding liposomes may be introduced in full-length TOR for future functional and localization studies in vivo.
激酶“雷帕霉素的靶标”的保守 C 端 FATC 结构域对其调节很重要，据推测它含有一个外周膜锚。在这里，我们通过 NMR 和 CD 光谱研究了酵母 TOR1 FATC 结构域（2438-2470=y1fatc）及其 15 个突变体与膜模拟胶束、双分子层脂囊泡和小单层囊泡（SUVs）的相互作用。取代多达 6-7 个残基不会导致与胶束或双分子层脂囊泡的结合显著丧失。然而，仅替换一个残基就可能导致与 SUV 的相互作用受损，而 SUV 通常在低浓度下使用。一些不结合脂质体的突变体可能被引入全长 TOR 中，用于未来的体内功能和定位研究。
