Toro-Nahuelpan Mauricio, Plitzko Jürgen M, Schüler Dirk, Pfeiffer Daniel
Department of Microbiology, University Bayreuth, Germany; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Planegg-Martinsried, Germany. Electronic address: https://twitter.com/Mauricio_Toro_N.
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Planegg-Martinsried, Germany.
J Mol Biol. 2022 Mar 15;434(5):167423. doi: 10.1016/j.jmb.2021.167423. Epub 2021 Dec 28.
The polar organizing protein Z (PopZ) forms a polar microdomain that is inaccessible to larger macromolecules such as ribosomes, and selectively sequesters proteins crucial for cell cycle control and polar morphogenesis in various Alphaproteobacteria. However, the in vivo architecture of this microdomain has remained elusive. Here, we analyzed the three-dimensional ultrastructural organization of the PopZ network in Magnetospirillum gryphiswaldense and Caulobacter crescentus by Volta phase plate cryo-electron tomography, which provides high spatial resolution and improved image contrast. Our results suggest that PopZ forms a porous network of disordered short, flexible, and branching filaments.
极性组织蛋白Z（PopZ）形成一个极性微结构域，核糖体等较大的大分子无法进入该结构域，并且它会选择性地隔离各种α-变形菌中对细胞周期控制和极性形态发生至关重要的蛋白质。然而，这个微结构域的体内结构仍然不清楚。在这里，我们通过伏打相板冷冻电子断层扫描分析了嗜磁螺菌和新月柄杆菌中PopZ网络的三维超微结构组织，该技术提供了高空间分辨率和改善的图像对比度。我们的结果表明，PopZ形成了一个由无序的短、柔性和分支细丝组成的多孔网络。
