Charting the native architecture of Chlamydomonas thylakoid membranes with single-molecule precision.
eLife 9:e53740 (2020)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
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Keywords
Chlamydomonas Reinhardtii ; Chloroplast ; Electron Microscopy ; In Situ ; Membranogram ; Molecular Biophysics ; Photosynthesis ; Plant Biology ; Structural Biology ; Thylakoid; Photosystem-ii; Chloroplast Membranes; Wild-type; Spatial-organization; Cytochrome B(6)f; Grana Margins; Higher-plants; Arrangement; Complexes; Dynamics
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Language
english
Publication Year
2020
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2020
ISSN (print) / ISBN
2050-084X
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2050-084X
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Volume: 9,
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Article Number: e53740
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eLife Sciences Publications
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Sheraton House, Castle Park, Cambridge, Cb3 0ax, England
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Peer reviewed
Institute(s)
Helmholtz Pioneer Campus (HPC)
POF-Topic(s)
30203 - Molecular Targets and Therapies
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Pioneer Campus
PSP Element(s)
G-510008-001
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Erfassungsdatum
2020-04-22