Charting the native architecture of Chlamydomonas thylakoid membranes with single-molecule precision

eLife

Dimitry Tegunov¹  Wolfgang Baumeister²  Miroslava Schaffer²  Sahradha Albert²  Jürgen M Plitzko²  Wojciech Wietrzynski³  Benjamin D Engel³  Atsuko Kanazawa⁴ 

[1] Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany;Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany;Helmholtz Pioneer Campus, Helmholtz Zentrum München, Neuherberg, Germany;Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany;MSU-DOE Plant Research Lab, Michigan State University, East Lansing, United States;

关键词: electron microscopy;    in situ;    photosynthesis;    chloroplast;    thylakoid;    membranogram;    Chlamydomonas reinhardtii;   

DOI  :  10.7554/eLife.53740

来源: publisher

【 摘 要 】

Thylakoid membranes scaffold an assortment of large protein complexes that work together to harness the energy of light. It has been a longstanding challenge to visualize how the intricate thylakoid network organizes these protein complexes to finely tune the photosynthetic reactions. Previously, we used in situ cryo-electron tomography to reveal the native architecture of thylakoid membranes (Engel et al., 2015). Here, we leverage technical advances to resolve the individual protein complexes within these membranes. Combined with a new method to visualize membrane surface topology, we map the molecular landscapes of thylakoid membranes inside green algae cells. Our tomograms provide insights into the molecular forces that drive thylakoid stacking and reveal that photosystems I and II are strictly segregated at the borders between appressed and non-appressed membrane domains. This new approach to charting thylakoid topology lays the foundation for dissecting photosynthetic regulation at the level of single protein complexes within the cell.

【 授权许可】

CC BY