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Gupta, T.K.* ; Klumpe, S.* ; Gries, K.* ; Heinz, S.* ; Wietrzynski, W. ; Ohnishi, N.* ; Niemeyer, J.* ; Spaniol, B.* ; Schaffer, M.* ; Rast, A.* ; Ostermeier, M.* ; Strauss, M.* ; Plitzko, J.M.* ; Baumeister, W.* ; Rudack, T.* ; Sakamoto, W.* ; Nickelsen, J.* ; Schuller, J.M.* ; Schroda, M.* ; Engel, B.D.

Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity.

Cell 184, 3643-3659.e23 (2021)
Verlagsversion Postprint DOI PMC
Open Access Green
Vesicle-inducing protein in plastids 1 (VIPP1) is essential for the biogenesis and maintenance of thylakoid membranes, which transform light into life. However, it is unknown how VIPP1 performs its vital membrane-remodeling functions. Here, we use cryo-electron microscopy to determine structures of cyanobacterial VIPP1 rings, revealing how VIPP1 monomers flex and interweave to form basket-like assemblies of different symmetries. Three VIPP1 monomers together coordinate a non-canonical nucleotide binding pocket on one end of the ring. Inside the ring's lumen, amphipathic helices from each monomer align to form large hydrophobic columns, enabling VIPP1 to bind and curve membranes. In vivo mutations in these hydrophobic surfaces cause extreme thylakoid swelling under high light, indicating an essential role of VIPP1 lipid binding in resisting stress-induced damage. Using cryo-correlative light and electron microscopy (cryo-CLEM), we observe oligomeric VIPP1 coats encapsulating membrane tubules within the Chlamydomonas chloroplast. Our work provides a structural foundation for understanding how VIPP1 directs thylakoid biogenesis and maintenance.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Chlamydomonas ; Clem ; Cryo-electron Tomography ; Cryo-em ; Escrt-iii ; Membrane Remodeling ; Nucleotide Hydrolysis ; Photosynthesis ; Stress Response ; Synechocystis ; Thylakoid Biogenesis; Cryo-em Structure; Shock-protein-a; Vesicle-inducing Protein; Beam-induced Motion; Escrt-iii; Phage-shock; Escherichia-coli; Cryoelectron Tomography; Molecular-dynamics; Bayesian-approach
Sprache englisch
Veröffentlichungsjahr 2021
HGF-Berichtsjahr 2021
ISSN (print) / ISBN 0092-8674
e-ISSN 1097-4172
Zeitschrift Cell
Quellenangaben Band: 184, Heft: 14, Seiten: 3643-3659.e23 Artikelnummer: , Supplement: ,
Verlag Cell Press
Verlagsort Cambridge, Mass.
Begutachtungsstatus Peer reviewed
Institut(e) Helmholtz Pioneer Campus (HPC)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Pioneer Campus
PSP-Element(e) G-510008-001
Förderungen LMU Munich's Institutional Strategy "LMU Excellent''
KAKENHI (Ministry of Education, Culture, Sports, Science and Technology)
KAKENHI (Japanese Society for the Promotion of Science)
Max Planck Society
Helmholtz Zentrum Munchen
Deutsche Forschungsgemeinschaft
DOI 10.1016/j.cell.2021.05.011
WOS ID WOS:000671212300008
Scopus ID 85108576636
PubMed ID 34166613
Erfassungsdatum 2021-07-05
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